>3608752 FitnessBrowser__Dino:3608752
MTLYSSGIAPVGTICDLRSDTVTRPCAGMRAAMADAEVGDDCYGEDPTVLRLEAVLAERTDKAAGLFFPTGCMSNLAALMAQCARGEEVIVGRDYHVYADEAASASVLGALSLVPIPVAEDGGLEPAEIRAALKPEDVHYARSRLLCLENTVGGRAVPLARMAAAVRTGREAGLSVHLDGARFFNAVTALGSSEAELAGLADTVSLCLSKGLGAPAGTVLVGPTPVIAEARRLRKLLGGGMRQSGVLAAAGLWALEHQLPRLAEDHARAARLARALIPLGTVRQGTNMVFFTPPVQNRAALAARMAGQGVRISDPGEGAIRLVVHRDVDDAALTAAIAAFESCL
>metacyc__MONOMER-12836 L-<i>allo</i>-threonine aldolase subunit (EC 4.1.2.48) (Aeromonas jandaei)
MRYIDLRSDTVTQPTDAMRQCMLHAEVGDDVYGEDPGVNALEAYGADLLGKEAALFVPSGTMSNLLAVMSHCQRGEGAVLGSAAHIYRYEAQGSAVLGSVALQPVPMQADGSLALADVRAAIAPDDVHFTPTRLVCLENTHNGKVLPLPYLREMRELVDEHGLQLHLDGARLFNAVVASGHTVRELVAPFDSVSICLSKGLGAPVGSLLVGSHAFIARARRLRKMVGGGMRQAGILAQAGLFALQQHVVRLADDHRRARQLAEGLAALPGIRLDLAQVQTNMVFLQLTSGESAPLLAFMKARGILFSGYGELRLVTHLQIHDDDIEEVIDAFTEYLGA
>biolip__3wgcB Aeromonas jandaei l-allo-threonine aldolase h128y/s292r double mutant
RYIDLRSDTVTQPTDAMRQCMLHAEVGDDVYGEDPGVNALEAYGADLLGKEAALFVPSGTMSNLLAVMSHCQRGEGAVLGSAAHIYRYEAQGSAVLGSVALQPVPMQADGSLALADVRAAIAPDDVYFTPTRLVCLENTHNGKVLPLPYLREMRELVDEHGLQLHLDGARLFNAVVASGHTVRELVAPFDSVSICLSKGLGAPVGSLLVGSHAFIARARRLRKMVGGGMRQAGILAQAGLFALQQHVVRLADDHRRARQLAEGLAALPGIRLDLAQVQTNMVFLQLTSGERAPLLAFMKARGILFSGELRLVTHLQIHDDDIEEVIDAFTEYL
>PDB_3wgb_D Crystal structure of aeromonas jandaei l-allo-threonine aldolase
YIDLRSDTVTQPTDAMRQCMLHAEVGDDVYGEDPGVNALEAYGADLLGKEAALFVPSGTMSNLLAVMSHCQRGEGAVLGS
AAHIYRYEAQGSAVLGSVALQPVPMDGSLALADVRAAIAPDDVHFTPTRLVCLENTHNGKVLPLPYLREMRELVDEHGLQ
LHLDGARLFNAVVASGHTVRELVAPFDSVSICLSKGLGAPVGSLLVGSHAFIARARRLRKMVGGGMRQAGILAQAGLFAL
QQHVVRLADDHRRARQLAEGLALPGIRLDLAQVQTNMVFLQLTSAPLLAFMKARGILFSELRLVTHLQIHDDDIEVIDAF
TEYL
>ecocyc__LTAA-MONOMER low-specificity L-threonine aldolase (EC 4.1.2.48; EC 4.1.2.5; EC 4.1.2.26; EC 4.1.2.49) (Escherichia coli K-12 substr. MG1655)
MIDLRSDTVTRPSRAMLEAMMAAPVGDDVYGDDPTVNALQDYAAELSGKEAAIFLPTGTQANLVALLSHCERGEEYIVGQAAHNYLFEAGGAAVLGSIQPQPIDAAADGTLPLDKVAMKIKPDDIHFARTKLLSLENTHNGKVLPREYLKEAWEFTRERNLALHVDGARIFNAVVAYGCELKEITQYCDSFTICLSKGLGTPVGSLLVGNRDYIKRAIRWRKMTGGGMRQSGILAAAGIYALKNNVARLQEDHDNAAWMAEQLREAGADVMRQDTNMLFVRVGEENAAALGEYMKARNVLINASPIVRLVTHLDVSREQLAEVAAHWRAFLAR
>PDB_3wlx_A Crystal structure of low-specificity l-threonine aldolase from escherichia coli
MIDLRSDTVTRPSRAMLEAMMAAPVGDDVYGDDPTVNALQDYAAELSGKEAAIFLPTGTQANLVALLSHCERGEEYIVGQ
AAHNYLFEAGGAAVLGSIQPQPIDAAADGTLPLDKVAMKIKPDDIHFARTKLLSLENTHNGKVLPREYLKEAWEFTRERN
LALHVDGARIFNAVVAYGCELKEITQYCDSFTICLSKGLGTPVGSLLVGNRDYIKRAIRWRKMTGGGMRQSGILAAAGIY
ALKNNVARLQEDHDNAAWMAEQLREAGADVMRQDTNMLFVRVGEENAAALGEYMKARNVLINASPIVRLVTHLDVSREQL
AEVAAHWRAFL
>biolip__4lnjA Structure of escherichia coli threonine aldolase in unliganded form
MIDLRSDTVTRPSRAMLEAMMAAPVGDDVYGDDPTVNALQDYAAELSGKEAAIFLPTGTQANLVALLSHCERGEEYIVGQAAHNYLFEAGGAAVLGSIQPQPIDAAADGTLPLDKVAMKIKPDDIHFARTKLLSLENTHNGKVLPREYLKEAWEFTRKRNLALHVDGARIFNAVVAYGCELKEITQYCDSFTICLSKGLGTPVGSLLVGNRDYIKRAIRWRKMTGGGMRQSGILAAAGMYALKNNVARLQEDHDNTAWMAEQLREAGADVMRQDTNMLFVRVGEENAAALGEYMKARNVLINASPIVRLVTHLDVSRAQLAEVAAHWRAFLA
>PDB_4lnm_A Structure of escherichia coli threonine aldolase in complex with serine
MIDLRSDTVTRPSRAMLEAMMAAPVGDDVYGDDPTVNALQDYAAELSGKEAAIFLPTGTQANLVALLSHCERGEEYIVGQ
AAHNYLFEAGGAAVLGSIQPQPIDAAADGTLPLDKVAMKIKPDDIHFARTKLLSLENTHNGKVLPREYLKEAWEFTRKRN
LALHVDGARIFNAVVAYGCELKEITQYCDSFTICLSKGLGTPVGSLLVGNRDYIKRAIRWRKMTGGGMRQSGILAAAGMY
ALKNNVARLQEDHDNTAWMAEQLREAGADVMRQDTNMLFVRVGEENAAALGEYMKARNVLINASPIVRLVTHLDVSRAQL
AEVAAHWRAFL
>PDB_4rjy_A Crystal structure of e. Coli l-threonine aldolase in complex with a non-covalently uncleaved bound l-serine substrate
MIDLRSDTVTRPSRAMLEAMMAAPVGDDVYGDDPTVNALQDYAAELSGKEAAIFLPTGTQANLVALLSHCERGEEYIVGQ
AAHNYLFEAGGAAVLGSIQPQPIDAAADGTLPLDKVAMKIKPDDIHFARTKLLSLENTHNGKVLPREYLKEAWEFTRKRN
LALHVDGARIFNAVVAYGCELKEITQYCDSFTICLSKGLGTPVGSLLVGNRDYIKRAIRWRKMTGGGMRQSGILAAAGMY
ALKNNVARLQEDHDNTAWMAEQLREAGADVMRQDTNMLFVRVGEENAAALGEYMKARNVLINASPIVRLVTHLDVSRAQL
AEVAAHWRAFLA
>PDB_4lnl_A Structure of escherichia coli threonine aldolase in complex with allo- thr
MIDLRSDTVTRPSRAMLEAMMAAPVGDDVYGDDPTVNALQDYAAELSGKEAAIFLPTGTQANLVALLSHCERGEEYIVGQ
AAHNYLFEAGGAAVLGSIQPQPIDAAADGTLPLDKVAMKIKPDDIHFARTKLLSLENTHNGKVLPREYLKEAWEFTRKRN
LALHVDGARIFNAVVAYGCELKEITQYCDSFTICLSKGLGTPVGSLLVGNRDYIKRAIRWRKMTGGGMRQSGILAAAGMY
ALKNNVARLQEDHDNTAWMAEQLREAGADVMRQDTNMLFVRVGEENAAALGEYMKARNVLINASPIVRLVTHLDVSRAQL
AEVAAHWRAFLA
>biolip__1jg8D Crystal structure of threonine aldolase (low-specificity)
MMIDLRSDTVTKPTEEMRKAMAQAEVGDDVYGEDPTINELERLAAETFGKEAALFVPSGTMGNQVSIMAHTQRGDEVILEADSHIFWYEVGAMAVLSGVMPHPVPGKNGAMDPDDVRKAIRPRNIHFPRTSLIAIENTHNRSGGRVVPLENIKEICTIAKEHGINVHIDGARIFNASIASGVPVKEYAGYADSVMFCLSKGLCAPVGSVVVGDRDFIERARKARKMLGGGMRQAGVLAAAGIIALTKMVDRLKEDHENARFLALKLKEIGYSVNPEDVKTNMVILRTDNLKVNAHGFIEALRNSGVLANAVSDTEIRLVTHKDVSRNDIEEALNIFEKLFRKFS
>BRENDA__Q9X266 L-threonine aldolase (EC 4.1.2.5) (Thermotoga maritima)
MIDLRSDTVTKPTEEMRKAMAQAEVGDDVYGEDPTINELERLAAETFGKEAALFVPSGTMGNQVSIMAHTQRGDEVILEADSHIFWYEVGAMAVLSGVMPHPVPGKNGAMDPDDVRKAIRPRNIHFPRTSLIAIENTHNRSGGRVVPLENIKEICTIAKEHGINVHIDGARIFNASIASGVPVKEYAGYADSVMFCLSKGLCAPVGSVVVGDRDFIERARKARKMLGGGMRQAGVLAAAGIIALTKMVDRLKEDHENARFLALKLKEIGYSVNPEDVKTNMVILRTDNLKVNAHGFIEALRNSGVLANAVSDTEIRLVTHKDVSRNDIEEALNIFEKLFRKFS
>PDB_1lw5_B X-ray structure of l-threonine aldolase (low-specificity) in complex with glycine
MIDLRSDTVTKPTEEMRKAMAQAEVGDDVYGEDPTINELERLAAETFGKEAALFVPSGTMGNQVSIMAHTQRGDEVILEA
DSHIFWYEVGAMAVLSGVMPHPVPGKNGAMDPDDVRKAIRPRNIHFPRTSLIAIENTHNRSGGRVVPLENIKEICTIAKE
HGINVHIDGARIFNASIASGVPVKEYAGYADSVMFCLSKGLCAPVGSVVVGDRDFIERARKARKMLGGGMRQAGVLAAAG
IIALTKMVDRLKEDHENARFLALKLKEIGYSVNPEDVKTNMVILRTDNLKVNAHGFIEALRNSGVLANAVSDTEIRLVTH
KDVSRNDIEEALNIFEKLFRKFS
>PDB_1lw4_B X-ray structure of l-threonine aldolase (low-specificity) in complex with l-allo-threonine
MIDLRSDTVTKPTEEMRKAMAQAEVGDDVYGEDPTINELERLAAETFGKEAALFVPSGTMGNQVSIMAHTQRGDEVILEA
DSHIFWYEVGAMAVLSGVMPHPVPGKNGAMDPDDVRKAIRPRNIHFPRTSLIAIENTHNRSGGRVVPLENIKEICTIAKE
HGINVHIDGARIFNASIASGVPVKEYAGYADSVMFCLSKGLCAPVGSVVVGDRDFIERARKARKMLGGGMRQAGVLAAAG
IIALTKMVDRLKEDHENARFLALKLKEIGYSVNPEDVKTNMVILRTDNLKVNAHGFIEALRNSGVLANAVSDTEIRLVTH
KDVSRNDIEEALNIFEKLFRKFS
>SwissProt__Q9FPH3 Probable low-specificity L-threonine aldolase 2; Threonine aldolase 2; EC 4.1.2.48 (Arabidopsis thaliana (Mouse-ear cress))
MVTPTTIRTVDLRSDTVTKPTESMRSAMANAEVDDDVLGNDPTALRLEKEVAEIAGKEAAMFVPSGTMGNLISVLVHCDERGSEVILGDDSHIHIYENGGVSSLGGVHPRTVKNEEDGTMEIGAIEAAVRSPKGDLHHPVTKLICLENTQANCGGRCLPIEYIDKVGELAKKHGLKLHIDGARIFNASVALGVPVKRIVQAADSVSICLSKGIGAPVGSVIVGSKKFITKARWLRKTLGGGMRQIGVLCAAALVALHENVAKLEDDHKKARVLAEGLNRIERLRVNVAAVETNIIYVDIPEDPKFGAEEACKSLEDVGVLVIPQATFRIRIVLHHQISDVDVEYVLSCFEKIFHS
>SwissProt__Q8RXU4 Low-specificity L-threonine aldolase 1; Threonine aldolase 1; EC 4.1.2.48 (Arabidopsis thaliana (Mouse-ear cress))
MVMRSVDLRSDTVTRPTDAMREAMCNAEVDDDVLGYDPTARRLEEEMAKMMGKEAALFVPSGTMGNLISVMVHCDVRGSEVILGDNCHIHVYENGGISTIGGVHPKTVKNEEDGTMDLEAIEAAIRDPKGSTFYPSTRLICLENTHANSGGRCLSVEYTEKVGEIAKRHGVKLHIDGARLFNASIALGVPVHKLVKAADSVQVCLSKGLGAPVGSVIVGSQSFIEKAKTVRKTLGGGMRQIGVLCAAALVALQENLPKLQHDHKKAKLLAEGLNQMKGIRVNVAAVETNMIFMDMEDGSRLTAEKLRKNLEENGILLIRGNSSRIRIVIHHQITTSDVHYTLSCFQQAMLTMQEPSRT
>CharProtDB__CH_090824 threonine aldolase; EC 4.1.2.5 (Saccharomyces cerevisiae)
MTEFELPPKYITAANDLRSDTFTTPTAEMMEAALEASIGDAVYGEDVDTVRLEQTVARMAGKEAGLFCVSGTLSNQIAIRTHLMQPPYSILCDYRAHVYTHEAAGLAILSQAMVVPVVPSNGDYLTLEDIKSHYVPDDGDIHGAPTRLISLENTLHGIVYPLEELVRIKAWCMENGLKLHCDGARIWNAAAQSGVPLKQYGEIFDSISICLSKSMGAPIGSVLVGNLKFVKKATHFRKQQGGGIRQSGMMARIALVNINNDWKSQLLYSHSLAHELAEYCEAKGIPLESPADTNFVFINLKAARMDPDVLVKKGLKYNVKLMGGRVSFHYQVTRDTLEKVKLAISEAFDYAKEHPFDCNGPTQIYRSESTEVDVDGNAIREIKTYKY
>metacyc__YEL046C-MONOMER L-threonine aldolase subunit (EC 4.1.2.48) (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
MTEFELPPKYITAANDLRSDTFTTPTAEMMEAALEASIGDAVYGEDVDTVRLEQTVARMAGKEAGLFCVSGTLSNQIAIRTHLMQPPYSILCDYRAHVYTHEAAGLAILSQAMVVPVVPSNGDYLTLEDIKSHYVPDDGDIHGAPTRLISLENTLHGIVYPLEELVRIKAWCMENGLKLHCDGARIWNAAAQSGVPLKQYGEIFDSISICLSKSMGAPIGSVLVGNLKFVKKATHFRKQQGGGIRQSGMMARMALVNINNDWKSQLLYSHSLAHELAEYCEAKGIPLESPADTNFVFINLKAARMDPDVLVKKGLKYNVKLMGGRVSFHYQVTRDTLEKVKLAISEAFDYAKEHPFDCNGPTQIYRSESTEVDVDGNAIREIKTYKY
>CharProtDB__CH_122707 hydroxytrimethyllysine aldolase (Candida albicans)
MDFSTFDKQSPAHNDFRSDTFTTPTTSMIQSLAQTTLGDAVYNEDLKTIELEQKVAELTGKEAGLYCVSGTLSNQIAIRTNLYQPPFSVLCDYRAHVYVHEAGGLSTLSQAMAQPINPKNGIHLTLEDDILPNFIIDDGEIHGAPTKLICLENTLHGMIFPIEEIKKISKFCQQNNVKLHLDGARIWNASAETGISLKEYCSYFDSVSLCLSKTLGAPIGTVLVSDKKFILKANHFKKQNGGGIRQSGLLASMAIIAIDENFSKLKQTHIWAKELGKLCDENGIILEHPVQTNFVFIDIAANKINPEKLIKISDKYNVKIYSGRIAFHYQISQESFENAKKVVLEVIQYAKDHPYEEKTNFKFYTSENK
>CharProtDB__CH_123166 L-threonine aldolase (Candida albicans)
MTADEEETFTTFNEFRSDTFTVPTRAMVEDGFMNATFGDSVYQEDETTLRLESKMCEITGKPAALFCVSGTMSNQIGLRANLVQPPYSILCDYRAHVFLHEAGGLATLSQAMVHPVRPSNGNYLTFEDVLANVTYDDGDIHAAPTKVISLENTLHGIIIPIEEIRKISEFCRENDIRLHLDGARLWNASVATGISIKEYCSYFDSVSLCLSKSLGAPIGSVLVGDEKFIRKANHFKKQSGGGIRQAGIMSAMAIHAIDYNLSKLELSHNYAKQIGDFCQEHGIKLESPVDTSLVFLDLKANKMDPNRLVELGRTKYNVKLMGQRIACHFQLSQESVDNVKKCILECFEYHQKHPHKDDGRNNKKMYSFDAIKK
>BRENDA__O13427 low-specificity L-threonine aldolase (EC 4.1.2.48) (Candida albicans)
MTADEEETFTTFNEFRSDTFTVPTRAMVEDGFMNATFGDSVYQEDETTLRLESKMCEITGKPAALFCVSGTMSNQIGLRANLVQPPYSILCDYRAHVFLHEAGGLATLSQAMVHPVRPSNGNYLTFEDVLGNVTYDDDGDIHAAPTKVISLENTLHGIIIPIEEIRKISEFCRENDIRLHLDGARLWNASVATGISIKEYCSYFDSVSLCLSKSLGAPIGSVLVGDEKFIRKANHFKKQSGGGIRQAGIMSAMAIHAIDYNLSKLELSHNYAKQIGDFCQEHGIKLESPVDTSLVFLDLKANKMDPNRLVELGRTKYNVKLMGQRIACHFQLSQESVDNVKKCILECLEYHQKHPHKDDGRNNKKMYSLDAIKK
>ENA__CAA06545.1 threonine aldolase (Eremothecium gossypii)
MNQDMELPEAYTSASNDFRSDTFTTPTREMIEAALTATIGDAVYQEDIDTLKLEQHVAKLAGMEAGMFCVSGTLSNQIALRTHLTQPPYSILCDYRAHVYTHEAAGLAILSQAMVTPVIPSNGNYLTLEDIKKHYIPDDGDIHGAPTKVISLENTLHGIIHPLEELVRIKAWCMENDLRLHCDGARIWNASAESGVPLKQYGELFDSISICLSKSMGAPMGSILVGSHKFIKKANHFRKQQGGGVRQSGMMCKMAMVAIQGDWKGKMRRSHRMAHELARFCAEHGIPLESPADTNFVFLDLQKSKMNPDVLVKKSLKYGCKLMGGRVSFHYQISEESLEKIKQAILEAFEYSKKNPYDENGPTKIYRSESADAVGEIKTYKY
>SwissProt__D7PHZ0 Aldolase vrtJ; Viridicatumtoxin synthesis protein J; EC 4.1.2.- (Penicillium aethiopicum)
MTNSPIADLVHHPERVQSPSLVNSKMNGDAKAVTEWTEPGPAAFDFRSDTVTRPTEQMLAAIAATTLQDDDFRQDPTTLGLEAWMAELTGKAAGLFVVSGTMGNQLGVRAHLQSPPHSVLCDARSHLVTHEAGGVASLSGAMVSCVTPVNGRYMTQADLEAHVNRGTLITDCPTRLVVLEIPLGGVILPLDKCRRISEWARAQGIALHLDGARLWEAVAAGAGSLRDYCACFDSVSLCFSKGLGAPIGSVLVGSETLRERARWIRKSIGGGMRQAGVVCAAARVAVEATFLGGLLKRSHARARDIATFWEIHGGRLTYPTETNMVWLDLEAVGWTPERLIRRGAELGLRFMGARLVVHYQIGDEAIGRLQDLMLEILVSGLVDHPRDS
>SwissProt__Q9UW18 Alanine racemase TOXG; TOX2 HC-toxin biosynthesis cluster protein TOXG; EC 5.1.1.1 (Cochliobolus carbonum (Maize leaf spot fungus) (Bipolaris zeicola))
MSNMVLNGNIDKSDRNSILDILQSLENIAWGQPGSARCDFRSDVITRPSLRMLSAVLKTTLGDDVFREDLTTAHFEAHVAEISGREEGMFVITGTMANQLCLHALVSTRPCGILLSSESHAIHYEAGGSSMLSGAMLQPVQPSNGKYLRVEDLEEHAILTDDVHKCPTSIVSMENTAGGAVVPVHELRRIRDWAKQNNVRTHLDGARLFEAVATGAGTLKEYCSLIDLVSVDFSKNLGAPMGAMILGDKKLIQQMRRTRKGIGGGMRQGGVITAAAREALFENFGLGAEIESQTLLQVHKVAKRLGEEWTRKGGKLSKEIETNIIWLDLDAVGIKKSQFIDKGREYGVILDGCRIVCHHQIDIYAVEALIDVFHDILKADPIKNKNSDR