>AO356_10230 AO356_10230 cysteine desulfhydrase
MIKEQLSRFNRLDLLSHPTPLEKLDRLSNWLGRDIYIKRDDLTPLALGGNKLRKLEYLAADAIAQGADTLITAGAIQSNHVRQTAALAAKLGLGCVALLENPIGTEDSNYLGNGNRLLLELFDAKVELVENLDNADEQLQALAGRLRSNGKKPYLVPIGGSNALGALGYVRAGLELAEQIKDTGIEFAAVVLASGSAGTHSGLALALSESLPALPVIGVTVSRSEEDQFPKVQGLAERTAALLEVALPEAFKVILWDEYFAPRYGEPNAGTLAAVKLLASLEGLLLDPVYTGKAVAGLLDGIGRDRFDEGPIIFLHTGGAPALFAYNTVF
>BRENDA__Q8ZNT7 D-cysteine desulfhydrase (EC 4.4.1.15) (Salmonella enterica subsp. enterica serovar Typhimurium)
MPLHHLTRFPRLEFIGAPTPLEYLPRLSDYLGREIYIKRDDVTPIAMGGNKLRKLEFLVADALREGADTLITAGAIQSNHVRQTAAVAAKLGLHCVALLENPIGTTAENYLTNGNRLLLDLFNTQIEMCDALTDPDAQLQTLATRIEAQGFRPYVIPVGGSSALGAMGYVESALEIAQQCEEVVGLSSVVVASGSAGTHAGLAVGLEHLMPDVELIGVTVSRSVAEQKPKVIALQQAIAGQLALTATADIHLWDDYFAPGYGVPNDAGMEAVKLLASLEGVLLDPVYTGKAMAGLIDGISQKRFNDDGPILFIHTGGAPALFAYHPHV
>biolip__4d8uH Crystal structure of d-cysteine desulfhydrase from salmonella typhimurium at 3.3 a in monoclinic space group with 8 subunits in the asymmetric unit
MASMPLHHLTRFPRLEFIGAPTPLEYLPRLSDYLGREIYIKRDDVTPIAMGGNKLRKLEFLVADALREGADTLITAGAIQSNHVRQTAAVAAKLGLHCVALLENPIGTTAENYLTNGNRLLLDLFNTQIEMCDALTDPDAQLQTLATRIEAQGFRPYVIPVGGSSALGAMGYVESALEIAQQCEEVVGLSSVVVASGSAGTHAGLAVGLEHLMPDVELIGVTVSRSVAEQKPKVIALQQAIAGQLALTATADIHLWDDYFAPGYGVPNDAGMEAVKLLASLEGVLLDPVYTGKAMAGLIDGISQKRFNDDGPILFIHTGGAPALFAYHPHV
>ecocyc__DCYSDESULF-MONOMER D-cysteine desulfhydrase (EC 4.4.1.15; EC 4.5.1.2) (Escherichia coli K-12 substr. MG1655)
MPLHNLTRFPRLEFIGAPTPLEYLPRFSDYLGREIFIKRDDVTPMAMGGNKLRKLEFLAADALREGADTLITAGAIQSNHVRQTAAVAAKLGLHCVALLENPIGTTAENYLTNGNRLLLDLFNTQIEMCDALTDPNAQLEELATRVEAQGFRPYVIPVGGSNALGALGYVESALEIAQQCEGAVNISSVVVASGSAGTHAGLAVGLEHLMPESELIGVTVSRSVADQLPKVVNLQQAIAKELELTASAEILLWDDYFAPGYGVPNDEGMEAVKLLARLEGILLDPVYTGKAMAGLIDGISQKRFKDEGPILFIHTGGAPALFAYHPHV
>PDB_4d9f_A D-cysteine desulfhydrase from salmonella typhimurium complexed with d- cycloserine (dcs)
MPLHHLTRFPRLEFIGAPTPLEYLPRLSDYLGREIYIKRDDVTPIAMGGNKLRKLEFLVADALREGADTLITAGAIQSNH
VRQTAAVAAKLGLHCVALLENPIGTTAENYLTNGNRLLLDLFNTQIEMCDALTDPDAQLQTLATRIEAQGFRPYVIPVGG
SSALGAMGYVESALEIAQQCEEVVGLSSVVVASGSAGTHAGLAVGLEHLMPDVELIGVTVSRSVAEQKPKVIALQQAIAG
QLALTATADIHLWDDYFAPGYGVPNDAGMEAVKLLASLEGVLLDPVYTGKAMAGLIDGISQKRFNDDGPILFIHTGGAPA
LFAYHPHV
>PDB_4d9e_A D-cysteine desulfhydrase from salmonella typhimurium complexed with l- cycloserine (lcs)
MPLHHLTRFPRLEFIGAPTPLEYLPRLSDYLGREIYIKRDDVTPIAMGGNKLRKLEFLVADALREGADTLITAGAIQSNH
VRQTAAVAAKLGLHCVALLENPIGTTAENYLTNGNRLLLDLFNTQIEMCDALTDPDAQLQTLATRIEAQGFRPYVIPVGG
SSALGAMGYVESALEIAQQCEEVVGLSSVVVASGSAGTHAGLAVGLEHLMPDVELIGVTVSRSVAEQKPKVIALQQAIAG
QLALTATADIHLWDDYFAPGYGVPNDAGMEAVKLLASLEGVLLDPVYTGKAMAGLIDGISQKRFNDDGPILFIHTGGAPA
LFAYHPHV
>PDB_4d9b_A Pyridoxamine 5' phosphate (pmp) bound form of salmonella typhimurium d-cysteine desulfhydrase obtained after co-crystallization with d- cycloserine
MPLHHLTRFPRLEFIGAPTPLEYLPRLSDYLGREIYIKRDDVTPIAMGGNKLRKLEFLVADALREGADTLITAGAIQSNH
VRQTAAVAAKLGLHCVALLENPIGTTAENYLTNGNRLLLDLFNTQIEMCDALTDPDAQLQTLATRIEAQGFRPYVIPVGG
SSALGAMGYVESALEIAQQCEEVVGLSSVVVASGSAGTHAGLAVGLEHLMPDVELIGVTVSRSVAEQKPKVIALQQAIAG
QLALTATADIHLWDDYFAPGYGVPNDAGMEAVKLLASLEGVLLDPVYTGKAMAGLIDGISQKRFNDDGPILFIHTGGAPA
LFAYHPHV
>PDB_4d99_A Salmonella typhimurium d-cysteine desulfhydrase with l-ser bound non- covalently at the active site
MPLHHLTRFPRLEFIGAPTPLEYLPRLSDYLGREIYIKRDDVTPIAMGGNKLRKLEFLVADALREGADTLITAGAIQSNH
VRQTAAVAAKLGLHCVALLENPIGTTAENYLTNGNRLLLDLFNTQIEMCDALTDPDAQLQTLATRIEAQGFRPYVIPVGG
SSALGAMGYVESALEIAQQCEEVVGLSSVVVASGSAGTHAGLAVGLEHLMPDVELIGVTVSRSVAEQKPKVIALQQAIAG
QLALTATADIHLWDDYFAPGYGVPNDAGMEAVKLLASLEGVLLDPVYTGKAMAGLIDGISQKRFNDDGPILFIHTGGAPA
LFAYHPHV
>PDB_4d97_A Salmonella typhimurium d-cysteine desulfhydrase with d-ser bound at active site
MPLHHLTRFPRLEFIGAPTPLEYLPRLSDYLGREIYIKRDDVTPIAMGGNKLRKLEFLVADALREGADTLITAGAIQSNH
VRQTAAVAAKLGLHCVALLENPIGTTAENYLTNGNRLLLDLFNTQIEMCDALTDPDAQLQTLATRIEAQGFRPYVIPVGG
SSALGAMGYVESALEIAQQCEEVVGLSSVVVASGSAGTHAGLAVGLEHLMPDVELIGVTVSRSVAEQKPKVIALQQAIAG
QLALTATADIHLWDDYFAPGYGVPNDAGMEAVKLLASLEGVLLDPVYTGKAMAGLIDGISQKRFNDDGPILFIHTGGAPA
LFAYHPHV
>PDB_4d96_A D-cysteine desulfhydrase from salmonella typhimurium complexed with 1- amino-1-carboxycyclopropane (acc)
MPLHHLTRFPRLEFIGAPTPLEYLPRLSDYLGREIYIKRDDVTPIAMGGNKLRKLEFLVADALREGADTLITAGAIQSNH
VRQTAAVAAKLGLHCVALLENPIGTTAENYLTNGNRLLLDLFNTQIEMCDALTDPDAQLQTLATRIEAQGFRPYVIPVGG
SSALGAMGYVESALEIAQQCEEVVGLSSVVVASGSAGTHAGLAVGLEHLMPDVELIGVTVSRSVAEQKPKVIALQQAIAG
QLALTATADIHLWDDYFAPGYGVPNDAGMEAVKLLASLEGVLLDPVYTGKAMAGLIDGISQKRFNDDGPILFIHTGGAPA
LFAYHPHV
>PDB_4d8w_A Salmonella typhimurium d-cysteine desulfhydrase soaked with d-cys shows pyruvate bound 4 a away from active site
MPLHHLTRFPRLEFIGAPTPLEYLPRLSDYLGREIYIKRDDVTPIAMGGNKLRKLEFLVADALREGADTLITAGAIQSNH
VRQTAAVAAKLGLHCVALLENPIGTTAENYLTNGNRLLLDLFNTQIEMCDALTDPDAQLQTLATRIEAQGFRPYVIPVGG
SSALGAMGYVESALEIAQQCEEVVGLSSVVVASGSAGTHAGLAVGLEHLMPDVELIGVTVSRSVAEQKPKVIALQQAIAG
QLALTATADIHLWDDYFAPGYGVPNDAGMEAVKLLASLEGVLLDPVYTGKAMAGLIDGISQKRFNDDGPILFIHTGGAPA
LFAYHPHV
>metacyc__MONOMER-15910 L-cysteate sulfo-lyase (EC 4.4.1.25) (Roseovarius nubinhibens (strain ATCC BAA-591 / DSM 15170 / ISM))
MHLARFPRRFIAHLPTPLERLDRLSAELGGPEIWIKRDDCTGLSTGGNKTRKLEFLMAEAELQGAEIVMTQGATQSNHARQTAAFAAKLGMKCHILLEDRTGSNEANYNHNGNVLLDHLHGATTEKRPGGGDMNAEMEKLADEWRADGKKVYTIPGGGSNPTGALGYVNCAFELLAQANDGGLKIDHIVHATGSAGTQAGLITGLKAMNAQIPLLGIGVRAPKPKQEENVYNLACATAEKLGCPGVVAREDVVANTDYVGQGYGIPTESGMEAIKMFAELESILLDPVYSAKGAAGFIDLIRKGHFKKGERVVFLHTGGAAALFGYDGAFDFSSRWVG
>BRENDA__C5AQP6 D-cysteine desulfhydrase (EC 4.4.1.15) (Methylorubrum extorquens)
MVLTRFPRVALTDGPTPIRSLDRLSTHLGPELNGVRLFVKRDDIGPVGLGGNKLRKLEFLLGQALAERADTVITVGALQSNHARLTAASAARMGLACELFLTRSVPREDADYTANGNRLLQDLFGAHVHLLPGEADSLAQAEARAEELRAEGRRVHVFPSGGSSPLGCLGYAACAAEILEQAANLGLAFARIVVPNGSSGTHAGLAAGLAAAGRDPHLAQSYTVLAPEPEAAAATLARARDTLALIDGSQTLADDAILVDGAHRGPGYGIPTEGMREAVRLMARTEGLLLDPVYSGKAFAGLLHDVRAGRYERGAAVLFVMTGGVPGLFAYRSEF
>metacyc__MONOMER-15876 L-cysteate sulfo-lyase subunit (EC 4.4.1.25) (Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3))
MHLARYPRRFIAHLPTPLERLDRLTAELGGPEIWIKRDDCTGLSTGGNKTRKLEFLMAEAELQGADMVMTQGATQSNHARQTAAFAAKLGMDCHILLEDRTGSNNANYNNNGNVLLDHLHGATTEKRPGSGLDMNAEMEKVAEKFRADGRKVYTIPGGGSNPTGALGYVNCAFEMLNQFNERGLKVDHIVHATGSAGTQAGLITGLQAMNAQIPLLGIGVRAPKPKQEENVYNLACATAEKLGCPGVVAREDVVANTDYVGEGYGIPTESGLEAIRMFAELEAILLDPVYSAKGAAGFIDLIRKGHFKKGERVVFLHTGGAVALFGYDNAFDYSGRWVA
>BRENDA__B8R7S1 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7) (Burkholderia cepacia)
MNLQRFPRYPLTFGPTPIQPLKRLSAHLGGKVELYAKREDCNSGLAFGGNKTRKLEYLVPDALAQGADTLVSIGGVQSNQTRQVAAVAAHLGMKCVLVQEHWVNYEDPVYDRVGNIQLSRMMGADVRLVADGFDIGIRRSWEEAMESVRQSGGKPYPIPAGCSEHPLGGLGFVGFAEEVREQEAQLGFKFDYIVVCSVTGSTQAGMVVGFAADGRADRVIGIDASATPERTHEQITRIARHTAELVGLGRDIETKDVVLDTRYAGPEYGLPNDGTLEAIRLCARLEGMLTDPVYEGKSMHGMIDKVQRGEFEPGSKVLYAHLGGVPALSAYAEIFRDG
>BRENDA__B8R7S5 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7) (Paraburkholderia silvatlantica)
MNLQRFPRYPLTFGPTPIQPLKRLSQHLGGKVELYAKREDCNSGLAFGGNKTRKLEYLIPDALAQGCDTLVSIGGIQSNQTRQVAAVAAHLGMKCVLVQENWVNYSDADYDRVGNIQMSRMMGADVRLVPDGFDIGIRPSWEEALESVRAAGGKPYAIPAGCSEHPFGGLGFVGFAEEVRAQEAQLGFKFDYIVVCSVTGSTQAGMVVGFAADGRADRVIGIDASATPQKTHAQITRIARHTAGLVDLNRDIGEKDVILDTRYGGPEYGLPNEGTLEAIRLCARLEGVLTDPVYEGKSMHGMIDKVRRGEFEPGSKVLYAHLGGVPALSAYSFIFRDG
>BRENDA__B1M5C5 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7) (Methylobacterium radiotolerans)
MLDKFERYPLTFGPTPIEPLKRLTAHLGGEVELYAKREDCNSGLAYGGNKLRKLEYIVPDAIASGADTLVSIGGVQSNHTRMVAAVAAKIGMKCRLIQEAWVPHEDAVYDRVGNILLSRIMGAQTQLVDDGFDIGIRDSWKRALAEVEAEGGKPYAIPAGASVHKYGGLGYVGFAEEVRKQEAEMGLRFDYVVVCTVTGSTHAGMLVGFSADGRARNVIGIDASCTPAQTKAQVLDIAQNTAALVGAGDIVADDVVLNEDYAYPVYGVPSKETVEAIRLSARLEGMITDPVYEGKSMQGMIDLVKKGFFPKGSKVLYAHLGGAPALNGYSYTFRNG
>BRENDA__B8R7S9 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7) (Burkholderia vietnamiensis)
MNLQRFPRYPLTFGPTPIQPLKHLSAHLGGKVELYAKREDCNSGLAFGGNKTRKLEYLIPDALAQGADTLVSIGGVQSNQTRQVAAVAAHLGMKCVLVQEHWVNYDDPVYDRVGNIQLSRMMGADVRLVADGFDIGIRRSWEDAMESVRQAGGKPYPIPAGCSEHPLGGLGFVGFAEEVREQEAQLGFRFDYVVVCSVTGSTQAGMVVGFAADGRADRVIGIDASATPERTREQITRIARHTAELVELGRPIADADVVLDTRYAGPEYGLPNDGTLEAIRLCARLEGVLTDPVYEGKSMHGMIDMVRRGEFEPGSKVLYAHLGGVPALSAYAEIFRNG
>BRENDA__B8R7S8 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7) (Paraburkholderia unamae)
MNLQRFPRYPLTFGPTPIQPLKRLSQHLGGKVELYAKREDCNSGLAFGGNKTRKLEYLIPDALAQGCDTLVSIGGIQSNQTRQVAAVAAHLGMKCVLVQENWVNYSDAVYDRVGNIQMSRMVGADVRLVADGFDIGIRPSWEEALESVRQAGGKPYAIPAGCSEHPLGGLGFVGFAEEVRQQEAELGFKFDYIVVCSVTGSTQAGMVVGFAADGRANRVIGIDASATPEKTHAQITRIARHTAGLVDLSRDIGEQDVTLDTRYGGPEYGLPNEGTLEAIRLCARMEGMLTDPVYEGKSMHGMIDKVRLGEFEPGSKVLYAHLGGVPALSAYSFIFRDG
>BRENDA__B2JYI5 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7) (Paraburkholderia phymatum)
MNLQRFARYPLTFGPTPIQPLKRLSQHLGGKVELYAKREDCNSGLAFGGNKTRKLEYLIPDALAQGCDTLVSIGGIQSNQTRQVAAVAAHLGMKCVLVQENWVNYYDAVYDRVGNIQMSRIMGADVRLVPDGFDIGIRKSWEEALDSVRAAGGKPYPIPAGCSEHPLGGLGFVGFAEEVRQQEAELGFRFDYIVVCSVTGSTQAGMIVGFAADGRADRVIGIDASAKSEQTREQITRIAKHTAERVDLGRDITAQDVVLDTRYGGPEYGLPNEGTLDAIRLCARLEGVMTDPVYEGKSMHGMIDKVRLGEFPEGSKVLYAHLGGVPALSAYSFIFRDG
>BRENDA__B4EJA6 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7) (Burkholderia cenocepacia)
MNLQRFPRYPLTFGPTPIQPLKRLSAHLGGKVELYAKREDCNSGLAFGGNKTRKLEYLVPDALAQGADTLVSIGGVQSNQTRQVAAVAAHLGMKCVLVQEHWVNYEDPVYDRVGNIQLSRMMGADVRLVADGFDIGIRRSWEEAMESVRQAGGKPYPIPAGCSEHPLGGLGFVGFAEEVRAQEAELGFRFDYVVVCSVTGSTQAGMVVGFAADGRADRVIGIDASAKPEQTREQITRIARHTAELVGLGRDIVERDVVLDTRYGGPEYGLPSDGTLEAIRLCARLEGMLTDPVYEGKSMHGMIDKVRLGEFEPGSKVLYAHLGGAPALSAYNGIFRNG
>BRENDA__B8R7S3 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7) (Paraburkholderia phenoliruptrix)
MNLQRFPRYPLTFGPTPIQPLKRLSDHLGGKVHLYAKREDCNSGFAFGGNKTRKLEYLIPEALAQGCDTLVSIGGIQSNQTRQVAAVAAHLGMKCVLVQENWVNYSDAVYDRVGNIQMSRILGADVRLVPDGFDIGFRKSWEDALESVRAAGGKPYAIPAGCSDHPLGGLGFVGFAEEVRQQEAELGFKFDYIVVCSVTGSTQAGMVVGFAADGRADRVIGIDASAKPAQTREQITRIASRTAEKVGLGRDITAQDVVLDERFGGPEYGLPNDGTLEAIRLCARLEGVLTDPVYEGKSMHGMIDMVRNDEFPEGSRVLYAHLGGVPALNGYSFIFRNG
>BRENDA__B8R7S7 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7) (Paraburkholderia terricola)
MNLQRFPRHPLTFGPTPIQPLKRLSDHLGGKVHLYAKREDCNSGFAFGGNKTRKLEYLIPEALAQGCDTLVSIGGIQSNQTRQVAAVAAHLGMKCVLVQENWVNYSDAVYDRVGNIQMSRILGADVRLVADGFDIGFRKSWEDALESVRAAGGKPYAIPAGCSDHPLGGLGFVGFAEEVRQQEAELGFKFDYIVVCSVTGSTQAGMVVGFAADGRAERVIGIDASAKPAQTREQIIRIAKQTAEKVELGRDITSKDVVLDERFGGPEYGLPNDGTLEAIRLCARLEGMLTDPVYEGKSMHGMIDMVRNGEFPEGSRVLYAHLGGVPALNGYSFIFRNG
>BRENDA__B8IP05 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7) (Methylobacterium nodulans)
MLEKFERYPLTFGPTPIERLGRLSAHLGGQVELYAKREDCNSGLAFGGNKLRKLEYIVPDAIASGADTLVSIGGVQSNHTRMVAAVAAKIGMKCRLVQEAWVPHEDAVYDRVGNIMLSRILGADVRLVDDGFDIGIRSSWQEAIDDVKAKGGRPYAIPAGASVHKFGGLGYVGFAEEVRAQERDLGFTFDYIVVCTVTGSTHAGMVVGFAKDGRERRVIGIDASATPAQTKAQVLDIARRTADLVGLGRDLSADDVVLNEDYAYPVYGVPSQETKDAIRLCARLEGMITDPVYEGKSMQGMIDLVRKGFFPAGSKVLYAHLGGAPALNGYGYTFRNG
>BRENDA__B8R7S2 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7) (Paraburkholderia graminis)
MNLQRFPRYPLTFGPTPIQPLKRLSDHLGGKVHLYAKREDCNSGFAFGGNKTRKLEYLIPEALAQGCDTLVSIGGIQSNQTRQVAAVAAHLGMKCVLVQENWVNYSDAVYDRVGNIQMSRILGADVRLVPDGFDIGFRKSWEDALESVRAAGGKPYAIPAGCSDHPLGGLGFVGFAEEVRQQEAELGFRFDYIVVCSVTGSTQAGMVVGFAADGRAERVIGIDASAKPAQTREQITRIARQTAEKVGLARDITAQDVVLDERFGGPEYGLPNAGTLEAIRLCARLEGVLTDPVYEGKSMHGMIDMVRNGEFPEGSRVLYAHLGGVPALNGYSFIFRNG
>BRENDA__Q89XR6 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7) (Bradyrhizobium japonicum)
MLEKFARYPLTFGPTPIEKLERLSKHLGGNVEIYAKREDCNSGLAYGGNKLRKLEYIIPDAIASNADTLVSIGGVQSNHTRMIAAVAAKIGMKCRLVQEAWVPHEDAVYDRVGNIMLSRIMGADVRLVDDGFDIGIRKSWEQAIEEVKAAGGKPYAIPAGASVHKYGGLGYVGFAEEVRKQEAELGFKFDYIVVCTVTGSTHAGMLVGFAADGRARKVIGIDGSFTPAQTKAQVLSIAQNTAKLVELGKDIVADDVVLIEDYAYPAYGVPSEETKEAIRLTARLEAMITDPVYEGKSMQGLIDLTQKGYFEKGAKVLYAHLGGAPALNGYGYAFRNG
>BRENDA__B2TBV3 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7) (Paraburkholderia phytofirmans)
MNLQRFPRYPLTFGPTPIQPLKRLSDHLGGKVHLYAKREDCNSGFAFGGNKTRKLEYLIPEALAQGCDTLVSIGGIQSNQTRQVAAVAAHLGMKCVLVQENWVNYSDAVYDRVGNIQMSRILGADVRLVADGFDIGFRKSWEDALESVRAAGGKPYAIPAGCSDHPLGGLGFVGFAEEVRQQEAELGFKFDYIVVCSVTGSTQAGMVVGFADDGRAERVIGIDASAKPAQTREQITRIAKQTAEQVGLGRDITSKDVVLDERFGGPEYGLPNDGTLEAIRLCARLEGVLTDPVYEGKSMHGMIEMVRNGEFPEGSRVLYAHLGGVPALNGYSFIFRNG
>BRENDA__B8R7R9 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7) (Paraburkholderia caledonica)
MNLQRFPRYPLTFGPTPIQPLKRLSDHLGGKVHLYAKREDCNSGFAFGGNKTRKLEYLIPEALAQGCDTLVSIGGIQSNQTRQVAAVAAHLGMKCVLVQENWVNYSDAVYDRVGNIQMSRILGADVRLVPDGFDIGFRKSWEDALESVRAAGGKPYAIPAGCSDHPLGGLGFVGFAEEVRQQEAELGFKFDYIVVCSVTGSTQAGMVVGFAADGRADRVIGIDASAKPAQTREQITRIASRTAEKVGLGRDIMAKDVVLDERFGGPEYGLPNDGTLQAIRLCARQEGVLTDPVYEGKSMHGMIDMVRNGEFPEGSRVLYAHLGGVPALNGYSFIFRNG
>SwissProt__Q5PWZ8 1-aminocyclopropane-1-carboxylate deaminase; ACC deaminase; ACCD; EC 3.5.99.7 (Pseudomonas putida (Arthrobacter siderocapsulatus))
MNLNRFERYPLTFGPSPITPLKRLSEHLGGKVELYAKREDCNSGLAFGGNKTRKLEYLIPEAIEQGCDTLVSIGGIQSNQTRQVAAVAAHLGMKCVLVQENWVNYSDAVYDRVGNIEMSRIMGADVRLDAAGFDIGIRPSWEKAMSDVVERGGKPFPIPAGCSEHPYGGLGFVGFAEEVRQQEKELGFKFDYIVVCSVTGSTQAGMVVGFAADGRSKNVIGVDASAKPEQTKAQILRIARHTAELVELGREITEEDVVLDTRFAYPEYGLPNEGTLEAIRLCGSLEGVLTDPVYEGKSMHGMIEMVRRGEFPDGSKVLYAHLGGAPALNAYSFLFRNG
>PDB_1tzm_A Crystal structure of acc deaminase complexed with substrate analog b- chloro-d-alanine
MNLQRFPRYPLTFGPTPIQPLARLSKHLGGKVHLYAKREDCNSGLAFGGNKTRKLEYLIPEALAQGCDTLVSIGGIQSNQ
TRQVAAVAAHLGMKCVLVQENWVNYSDAVYDRVGNIQMSRILGADVRLVPDRSWEDALESVRAAGGKPYAIPAGCSDHPL
GGLGFVGFAEEVRAQEAELGFKFDYVVVCSVTGSTQAGMVVGFAADGRADRVIGVDASAKPAQTREQITRIARQTAEKVG
LERDIMRADVVLDERFAGPEYGLPNEGTLEAIRLCARTEGMLTDPVYEGKSMHGMIEMVRNGEFPEGSRVLYAHLGGVPA
LNGYSFIFRDG
>PDB_1tzk_A Crystal structure of 1-aminocyclopropane-1-carboxylate-deaminase complexed with alpha-keto-butyrate
MNLQRFPRYPLTFGPTPIQPLARLSKHLGGKVHLYAKREDCNSGLAFGGNKTRKLEYLIPEALAQGCDTLVSIGGIQSNQ
TRQVAAVAAHLGMKCVLVQENWVNYSDAVYDRVGNIQMSRILGADVRLVPDRSWEDALESVRAAGGKPYAIPAGCSDHPL
GGLGFVGFAEEVRAQEAELGFKFDYVVVCSVTGSTQAGMVVGFAADGRADRVIGVDASAKPAQTREQITRIARQTAEKVG
LERDIMRADVVLDERFAGPEYGLPNEGTLEAIRLCARTEGMLTDPVYEGKSMHGMIEMVRNGEFPEGSRVLYAHLGGVPA
LNGYSFIFRDG
>PDB_1tzj_A Crystal structure of 1-aminocyclopropane-1-carboxylate deaminase complexed with d-vinyl glycine
MNLQRFPRYPLTFGPTPIQPLARLSKHLGGKVHLYAKREDCNSGLAFGGNKTRKLEYLIPEALAQGCDTLVSIGGIQSNQ
TRQVAAVAAHLGMKCVLVQENWVNYSDAVYDRVGNIQMSRILGADVRLVPDRSWEDALESVRAAGGKPYAIPAGCSDHPL
GGLGFVGFAEEVRAQEAELGFKFDYVVVCSVTGSTQAGMVVGFAADGRADRVIGVDASAKPAQTREQITRIARQTAEKVG
LERDIMRADVVLDERFAGPEYGLPNEGTLEAIRLCARTEGMLTDPVYEGKSMHGMIEMVRNGEFPEGSRVLYAHLGGVPA
LNGYSFIFRDG
>PDB_1tz2_A Crystal structure of 1-aminocyclopropane-1-carboyxlate deaminase complexed with acc
MNLQRFPRYPLTFGPTPIQPLARLSKHLGGKVHLYAKREDCNSGLAFGGNKTRKLEYLIPEALAQGCDTLVSIGGIQSNQ
TRQVAAVAAHLGMKCVLVQENWVNYSDAVYDRVGNIQMSRILGADVRLVPDRSWEDALESVRAAGGKPYAIPAGCSDHPL
GGLGFVGFAEEVRAQEAELGFKFDYVVVCSVTGSTQAGMVVGFAADGRADRVIGVDASAKPAQTREQITRIARQTAEKVG
LERDIMRADVVLDERFAGPEYGLPNEGTLEAIRLCARTEGMLTDPVYEGKSMHGMIEMVRNGEFPEGSRVLYAHLGGVPA
LNGYSFIFRDG
>BRENDA__C3VP48 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7) (Pseudomonas entomophila)
MNLNRFKRYPLTFGPSPITPLKRLSEHLGGKVELYAKREDCNSGLAFGGNKTRKLEYLIPEAIEQGCDTLVSIGGTQSNQTRQVAAVAAHLGMKCVLVQENWVNYSDAVYDRVGNIEMSRIMGADVRLDAAGFDIGIRPSWEKAMSDVVERGGKPFPIPAGCSEHPYGGLGFVGFAEEVRQQEKELGFKFDYIVVCSVTGSTQAGMVVGFAADGRSKNVIGVDASAKPEQTKAQILRIARHTAELVELGREITEEDVVLDTRFAYPEYGLPNEGTLEAIRLCGSLEGVLTDPVYEGKSMHGMIEMVRRGEFPDGSKVLYAHLGGAPALNAYSFLFRNG
>SwissProt__Q00740 1-aminocyclopropane-1-carboxylate deaminase; ACC deaminase; ACCD; EC 3.5.99.7 (Pseudomonas sp. (strain ACP))
MNLQRFPRYPLTFGPTPIQPLARLSKHLGGKVHLYAKREDCNSGLAFGGNKTRKLEYLIPEALAQGCDTLVSIGGIQSNQTRQVAAVAAHLGMKCVLVQENWVNYSDAVYDRVGNIQMSRILGADVRLVPDGFDIGFRRSWEDALESVRAAGGKPYAIPAGCSDHPLGGLGFVGFAEEVRAQEAELGFKFDYVVVCSVTGSTQAGMVVGFAADGRADRVIGVDASAKPAQTREQITRIARQTAEKVGLERDIMRADVVLDERFAGPEYGLPNEGTLEAIRLCARTEGMLTDPVYEGKSMHGMIEMVRNGEFPEGSRVLYAHLGGVPALNGYSFIFRDG
>BRENDA__B8R7T2 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7) (Paraburkholderia xenovorans)
MNLQRFPRYPLTFGPTPIQPLARLSKHLGGKVHLYAKREDCNSGLAFGGNKTRKLEYLIPEVLAQGCDTLVSIGGIQSNQTRQVAAVAAHLGMKCVLVQENWVNYSDAVYDRVGNIQMSRILGADVRLVPDGFDIGFRKSWEEALESVRAAGGKPYAIPAGCSDHPLGGLGFVGFAEEVRRQEAELGFKFDYVVVCSVTGSTQPGMVGGFAADGRADRVIGIDASAKPAQTREQITRIARQTAEKVGLGRDITSEDVVLDERFAGPEYGLPNDGTLEAIRLCARMEGVLTDPVYEGKSMHGMIEMVRNGEFPEGSRVLYAHLGGVPALNGYSFIFRNG
>BRENDA__O57809 L-serine ammonia-lyase (EC 4.3.1.17); D-Serine ammonia-lyase (EC 4.3.1.18) (Pyrococcus horikoshii)
MHPKIFALLAKFPRVELIPWETPIQYLPNISREIGADVYIKRDDLTGLGIGGNKIRKLEYLLGDALSKGADVVITVGAVHSNHAFVTGLAAKKLGLDAILVLRGKEELKGNYLLDKIMGIETRVYDAKDSFELMKYAEEIAEELKREGRKPYVIPPGGASPIGTLGYVRAVGEIATQSEVKFDSIVVAAGSGGTLAGLSLGLSILNEDIRPVGIAVGRFGEVMTSKLDNLIKEAAELLGVKVEVRPELYDYSFGEYGKITGEVAQIIRKVGTREGIILDPVYTGKAFYGLVDLARKGELGEKILFIHTGGISGTFHYGDKLLSLL
>BRENDA__A8VU64 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7) (Sinorhizobium sp. BL3)
MSLLEKFQRYPLTFGPTPIEHLPRLTAALGGKVEIYAKREDCNSGLAMGGNKLKKLEYIVPDAIASGADTLVSIGGVQSNHTRMVAATAAKIGMKCVVIQEKWVPHYDAIYDRVGNILMTRLMGADSRLVDDGFDIGLRKSWEDAIQSVKDAGGKPYPIPAGASVHKLGALGYVGFAEEVAAQEKELGFTFDYIIVCVVTGSTQGGMIVGFAAQDRAERVIGIDASGTLDQTRAQVRKIVDATAELVGLNRAIQESEIIINPDYAYPAYGVPSDETNEAIRLAARTEAMITDPVYEGKSMQGMIDLTRKGFFPEGSKVLYAHLGGAPALNGYSYYYRDG
>PDB_1j0b_A Crystal structure analysis of the acc deaminase homologue complexed with inhibitor
MHPKIFALLAKFPRVELIPWETPIQYLPNISREIGADVYIKRDDLTGLGIGGNKIRKLEYLLGDALSKGADVVITVGAVH
SNHAFVTGLAAKKLGLDAILVLRGKEELKGNYLLDKIMGIETRVYDAKDSFELMKYAEEIAEELKREGRKPYVIPPGGAS
PIGTLGYVRAVGEIATQSEVKFDSIVVAAGSGGTLAGLSLGLSILNEDIRPVGIAVGRFGEVMTSKLDNLIKEAAELLGV
KVEVRPELYDYSFGEYGKITGEVAQIIRKVGTREGIILDPVYTGKAFYGLVDLARKGELGEKILFIHTGGISGTFHYGDK
LLSLL
>BRENDA__Q93AG0 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7) (Rhizobium leguminosarum)
MSLLEKFERYPLTFGPTPIEHLPRLTAALGGKVDIYAKRDDCNSGLAMGGNKLRKLEYIVPDAIASGADTLVSIGGVQSNHTRMVAATAAKIGMKCVVIQEKWVPHYDAVYDRVGNILMTKLMGADSRLVEDGFDIGIRKSWEDAIQSVEDAGGKPYAIPAGASVHKFGGLGYVGFAEEVAAQEKDLGFIFDYIIVCVVTGSTQGGMIVGFAALDRADRVIGIDASGTLQQTRDQVRKIVDATSELVNLGRSVREDEIVINPDYAYPAYGVPSEETNEAIRLAARTEAMITDPVYEGKSMQGMIDLARKGFFPEGSKVLYAHLGGAPALNGYSYYYKDG
>BRENDA__G5AFQ7 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7) (Phytophthora sojae)
MKLSKFAKHALTFSGPSPIQHLERLSKALGNKVQLYAKREDCNSGLAFGGNKTRKLEYIIPEAIEGGYDTLVSIGGIQSNQTRQVAAVAAHLGFKCVLVQENWVNYPPEEAPVYDNVGNIELSRILGADVRRDAAGFDIGIRPSWEAAMESVKKAGGKPYPIPAGCSEHPKGGLGFVDFAEEVRQQEKELGFKFDYIVVCAVTGSTMAGMVVGFAADGRANKVIGIDASATPEKTREQVLRIAKNTAELVELGRDITSDDVVLDTRFGGPEYGLPNQGTLDAIRLCARTEGMLTDPVYEGKSMDGMISMVRNGEFPEGSNVLYAHLGGAPALSAYSYLFKEG
>BRENDA__D3U2Q8 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7) (Trichoderma asperellum)
MATLNIPEPLASIPFESLLFGPSPIQHLPRISAALGGKVTVYAKRDDCNSGFAYGGNKVRKLEYLAAEALSQGCDTLVSIGGVQSNHTRAVTAVAAKLGLKAATVQEHWVDWDDAGYEKVGNIQLSRLMGGDVRLDPSLFGIEHKPTLANLKAELEGSGRKPYYIPAGASDHPLGGLGFARWALEVEAQEKEMGVFFDTVIVCAVTGSTMAGMIAGFKLAQLKLGSPKRKIIGIDASGKPKETFDQVLRIAKFTAAKIGLSEADITEADVILDERFNAKIYGIPDETTIEAMKFGARTEAFITDPVYEGKSLAGMMGLIRNGEIAGGNVLYAHLGGQLALNAYSSLLD
>biolip__1f2dA 1-aminocyclopropane-1-carboxylate deaminase
AGVAKFAKYPLTFGPSPISNLNRLSQHLGSKVNVYAKREDCNSGLAFGGNKLRKLEYIVPDIVEGDYTHLVSIGGRQSNQTRMVAALAAKLGKKCVLIQEDWVPIPEAEKDVYNRVGNIELSRIMGADVRVIEDGFDIGMRKSFANALQELEDAGHKPYPIPAGCSEHKYGGLGFVGFADEVINQEVELGIKFDKIVVCCVTGSTTAGILAGMAQYGRQDDVIAIDASFTSEKTKEQTLRIANNTAKLIGVEHEFKDFTLDTRFAYPCYGVPNEGTIEAIRTCAEQEGVLTDPVYEGKSMQGLIALIKEDYFKPGANVLYVHLGGAPALSAYSSFFPTKTA
>SwissProt_Q7M523 1-aminocyclopropane-1-carboxylate deaminase; ACC deaminase; ACCD; EC 3.5.99.7 from Cyberlindnera saturnus (Yeast) (Williopsis saturnus)
SGVAKFAKYPLTFGPSPISNLNRLSQHLGSKVNVYAKREDCNSGLAFGGNKLRKLEYIVPDIVEGDYTHLVSIGGRQSNQ
TRMVAALAAKLGKKCVLIQEDWVPIPEAEKDVYNRVGNIELSRIMGADVRVIEDGFDIGMRKSFANALQELEDAGHKPYP
IPAGCSEHKYGGLGFVGFADEVINQEVELGIKFDKIVVCCVTGSTTAGILAGMAQYGRQDDVIAIDASFTSEKTKEQTLR
IANNTAKLIGVEHEFKDFTLDTRFAYPCYGVPNEGTIEAIRTCAEQEGVLTDPVYEGKSMQGLIALIKEDYFKPGANVLY
VHLGGAPALSAYSSFFPTKTA
>PDB_1j0e_A Acc deaminase mutant reacton intermediate
AGVAKFAKYPLTFGPSPISNLNRLSQHLGSKVNVYAKREDCNSGLAFGGNKLRKLEYIVPDIVEGDYTHLVSIGGRQSNQ
TRMVAALAAKLGKKCVLIQEDWVPIPEAEKDVYNRVGNIELSRIMGADVRVIEDGFDIGMRKSFANALQELEDAGHKPYP
IPAGCSEHKYGGLGFVGFADEVINQEVELGIKFDKIVVCCVTGSTTAGILAGMAQYGRQDDVIAIDASFTSEKTKEQTLR
IANNTAKLIGVEHEFKDFTLDTRFAYPCYGVPNEGTIEAIRTCAEQEGVLTDPVFEGKSMQGLIALIKEDYFKPGANVLY
VHLGGAPALSAYSSFFPTKTA
>PDB_1j0d_A Acc deaminase mutant complexed with acc
AGVAKFAKYPLTFGPSPISNLNRLSQHLGSKVNVYAKREDCNSGLAFGGNTLRKLEYIVPDIVEGDYTHLVSIGGRQSNQ
TRMVAALAAKLGKKCVLIQEDWVPIPEAEKDVYNRVGNIELSRIMGADVRVIEDGFDIGMRKSFANALQELEDAGHKPYP
IPAGCSEHKYGGLGFVGFADEVINQEVELGIKFDKIVVCCVTGSTTAGILAGMAQYGRQDDVIAIDASFTSEKTKEQTLR
IANNTAKLIGVEHEFKDFTLDTRFAYPCYGVPNEGTIEAIRTCAEQEGVLTDPVYEGKSMQGLIALIKEDYFKPGANVLY
VHLGGAPALSAYSSFFPTKTA
>BRENDA__B2MWN0 D-cysteine desulfhydrase (EC 4.4.1.15) (Solanum lycopersicum)
MSSCQWSSFTRVSLSPFPLQPAQLNTALNLKKQCCFTKSSMEDSSSQGHQSAFQFLTKKPYEPPPWASLLSPIPSHTFSLGHFPTPIHKWNLPNLPKNTEVWLKRDDMSGMQLSGNKVRKLEFLLADAVAQGADCIVTIGGIQSNHCRATAVAAKYLNLDCYLILRTSKLLVDKDPGLTGNLLVDRLVGAHIDLVSKEEYAKVGGEALTKILKEKLLNEGRKPYVIPVGGSNSLGTWGYIEAIRELEQQLQHLSIEQKFDDIVVACGSGGTVAGLSIASMLSGLKAKINAFCVCDDPDYFYEYVQGLLDGITAGVSSRDIVSIKTAKGLGYALSTTDELKFVKQVAETTGVILDPVYSGKAAYGMMKDMGENPTKWEGRKILFIHTGGLLGLYDKADEIGSLMGKWRKMDINESIPRQDGIGKMF
>SwissProt__Q6ZHE5 D-cysteine desulfhydrase 1, mitochondrial; OsDCD1; OsD-CDes1; D-CDes1; EC 4.4.1.15 (Oryza sativa subsp. japonica (Rice))
MARGAHQAPGGFWTVAAAPTRCSLPHSLPIPLHAAAAAAAWMAGVSAASAAGKIGSFLSKRPYAPPSWASHLSPAPSQTFSLGHFPTPIHKWNLPNLPNGTEVWIKRDDISGMQLSGNKVRKLEFLMADAVAQGADCVITVGGIQSNHCRATAVAAKYINLDCYLILRTSKLLVDKDPGLVGNLLVERLVGAHIDLVSKEEYGKIGSVALADLLKKKLLEEGRKPYVIPVGGSNSLGTWGYIEAIREIEHQIQISGDVQFDDIVVACGSGGTIAGLALGSKLSSLKAKVHAFSVCDDPGYFHSYVQDLIDGLHSDLRSHDLVNIENAKGLGYAMNTAEELKFVKDIATATGIVLDPVYSGKAAYGMLKDMGANPAKWEGRKILFVHTGGLLGLYDKVDELSSLSGSWRRMDLEESVPRKDGTGKMF
>SwissProt__F4HYF3 Bifunctional D-cysteine desulfhydrase/1-aminocyclopropane-1-carboxylate deaminase, mitochondrial; 1-aminocyclopropane-1-carboxylic acid deaminase 1; AtACD1; AtD-CDes1; D-CDes1; D-CDES; EC 3.5.99.7; EC 4.4.1.15 (Arabidopsis thaliana (Mouse-ear cress))
MRGRSLTLSRVKLELARRSMSATSVPSMADFLTKKPYSPPSWASHLRPLPSHTFSLAHLPTPIHRWNLPGLPNGTELWIKRDDFTGMELSGNKVRKLEFLMAEAVDQHADTVITIGGIQSNHCRATATASNYLNLNSHLILRTSKLLADEDPGLVGNLLVERLVGANVHLISKEEYSSIGSEALTNALKEKLEKEGKKPYVIPVGGSNSLGTWGYIEAAREIEEQLNYRPDDLKFDDIVVACGSGGTIAGISLGSWLGALKAKVHAFSVCDDPDYFYDFVQGLLDGLHAGVNSRDIVNIHNAKGKGYAMNTSEELEFVKKVASSTGVILDPVYSGKAAYGLINEITKDPKCWEGRKILFIHTGGLLGLYDKVDQMASLMGNWSRMDVSESVPRKDGVGKMF