SitesBLAST
Comparing HSERO_RS00035 FitnessBrowser__HerbieS:HSERO_RS00035 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
5g4jA Phospholyase a1rdf1 from arthrobacter in complex with phosphoethanolamine (see paper)
42% identity, 93% coverage: 28:436/442 of query aligns to 2:415/423 of 5g4jA
- active site: S14 (≠ V40), Y130 (= Y156), D201 (= D223), D234 (= D256), Q237 (= Q259), K264 (= K286), T294 (= T316), K395 (= K416)
- binding {5-hydroxy-6-methyl-4-[(E)-{[2-(phosphonooxy)ethyl]imino}methyl]pyridin-3-yl}methyl dihydrogen phosphate: Y44 (= Y70), R73 (= R99), G103 (= G129), S104 (≠ T130), Y130 (= Y156), H131 (= H157), D234 (= D256), V236 (= V258), Q237 (= Q259), K264 (= K286), T294 (= T316), R397 (= R418)
5g4iA Plp-dependent phospholyase a1rdf1 from arthrobacter aurescens tc1 (see paper)
42% identity, 93% coverage: 28:436/442 of query aligns to 2:415/423 of 5g4iA
- active site: S14 (≠ V40), Y130 (= Y156), D201 (= D223), D234 (= D256), Q237 (= Q259), K264 (= K286), T294 (= T316), K395 (= K416)
- binding pyridoxal-5'-phosphate: G103 (= G129), S104 (≠ T130), H131 (= H157), D234 (= D256), V236 (= V258), Q237 (= Q259), K264 (= K286)
- binding phosphate ion: Y44 (= Y70), R397 (= R418)
6torB Human o-phosphoethanolamine phospho-lyase (see paper)
42% identity, 89% coverage: 48:439/442 of query aligns to 1:394/404 of 6torB
4ysnC Structure of aminoacid racemase in complex with plp (see paper)
31% identity, 88% coverage: 53:439/442 of query aligns to 41:438/448 of 4ysnC
- active site: Y149 (= Y156), E224 (≠ D223), D257 (= D256), N260 (≠ Q259), K287 (= K286), T316 (≠ N315), R415 (≠ K416)
- binding pyridoxal-5'-phosphate: S121 (= S128), G122 (= G129), S123 (≠ T130), Y149 (= Y156), H150 (= H157), E224 (≠ D223), D257 (= D256), V259 (= V258), K287 (= K286), F315 (= F314), T316 (≠ N315)
Sites not aligning to the query:
5wyaA Structure of amino acid racemase, 2.65 a (see paper)
31% identity, 88% coverage: 53:439/442 of query aligns to 32:429/439 of 5wyaA
- active site: Y140 (= Y156), E215 (≠ D223), D248 (= D256), N251 (≠ Q259), K278 (= K286), T307 (≠ N315), R406 (≠ K416)
- binding (2S,3S)-3-methyl-2-[[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]pentanoic acid: A52 (≠ N71), Y82 (= Y100), S112 (= S128), G113 (= G129), S114 (≠ T130), Y140 (= Y156), H141 (= H157), E215 (≠ D223), D248 (= D256), V250 (= V258), N251 (≠ Q259), K278 (= K286), F306 (= F314), T307 (≠ N315), R406 (≠ K416)
Sites not aligning to the query:
5wyfA Structure of amino acid racemase, 2.12 a (see paper)
31% identity, 88% coverage: 53:439/442 of query aligns to 34:431/446 of 5wyfA
- active site: Y142 (= Y156), E217 (≠ D223), D250 (= D256), N253 (≠ Q259), K280 (= K286), T309 (≠ N315), R408 (≠ K416)
- binding n-[o-phosphono-pyridoxyl]-isoleucine: A54 (≠ N71), Y84 (= Y100), G115 (= G129), S116 (≠ T130), Y142 (= Y156), H143 (= H157), D222 (≠ S228), D250 (= D256), V252 (= V258), N253 (≠ Q259), K280 (= K286), F308 (= F314), T309 (≠ N315), R408 (≠ K416)
Sites not aligning to the query:
1szkA The structure of gamma-aminobutyrate aminotransferase mutant: e211s (see paper)
30% identity, 94% coverage: 24:437/442 of query aligns to 2:422/425 of 1szkA
- active site: V18 (= V40), Y137 (= Y156), E205 (≠ D223), D238 (= D256), Q241 (= Q259), K267 (= K286), T296 (= T316), R397 (≠ K416)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G110 (= G129), S111 (≠ T130), Y137 (= Y156), H138 (= H157), E205 (≠ D223), D238 (= D256), V240 (= V258), Q241 (= Q259), K267 (= K286)
P42588 Putrescine aminotransferase; PAT; PATase; Cadaverine transaminase; Diamine transaminase; Putrescine transaminase; Putrescine--2-oxoglutaric acid transaminase; Putrescine:2-OG aminotransferase; EC 2.6.1.82; EC 2.6.1.29 from Escherichia coli (strain K12) (see paper)
30% identity, 89% coverage: 48:439/442 of query aligns to 66:449/459 of P42588
- GT 150:151 (= GT 129:130) binding in other chain
- Q274 (= Q259) binding in other chain
- K300 (= K286) modified: N6-(pyridoxal phosphate)lysine
- T332 (= T316) binding
4uoxC Crystal structure of ygjg in complex with pyridoxal-5'-phosphate and putrescine (see paper)
30% identity, 89% coverage: 48:439/442 of query aligns to 64:447/456 of 4uoxC
- active site: F178 (≠ Y156), E236 (≠ D223), D269 (= D256), Q272 (= Q259), K298 (= K286), T330 (= T316), R424 (≠ K416)
- binding pyridoxal-5'-phosphate: S147 (= S128), G148 (= G129), T149 (= T130), F178 (≠ Y156), H179 (= H157), G180 (= G158), D269 (= D256), V271 (= V258), Q272 (= Q259), K298 (= K286), T329 (≠ N315), T330 (= T316)
Sites not aligning to the query:
4uoxA Crystal structure of ygjg in complex with pyridoxal-5'-phosphate and putrescine (see paper)
30% identity, 89% coverage: 48:439/442 of query aligns to 60:443/453 of 4uoxA
- active site: F174 (≠ Y156), E232 (≠ D223), D265 (= D256), Q268 (= Q259), K294 (= K286), T326 (= T316), R420 (≠ K416)
- binding pyridoxal-5'-phosphate: S143 (= S128), G144 (= G129), T145 (= T130), F174 (≠ Y156), H175 (= H157), G176 (= G158), D265 (= D256), V267 (= V258), Q268 (= Q259), T325 (≠ N315), T326 (= T316)
- binding 1,4-diaminobutane: E237 (≠ S228), K294 (= K286)
Sites not aligning to the query:
1sffA Structure of gamma-aminobutyrate aminotransferase complex with aminooxyacetate (see paper)
30% identity, 94% coverage: 24:437/442 of query aligns to 2:422/425 of 1sffA
- active site: V18 (= V40), Y137 (= Y156), E205 (≠ D223), D238 (= D256), Q241 (= Q259), K267 (= K286), T296 (= T316), R397 (≠ K416)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: Q78 (≠ L101), G110 (= G129), S111 (≠ T130), Y137 (= Y156), H138 (= H157), R140 (≠ H159), E205 (≠ D223), D238 (= D256), V240 (= V258), Q241 (= Q259), K267 (= K286), T296 (= T316)
- binding sulfate ion: N152 (≠ G171), Y393 (≠ G412)
1sf2A Structure of e. Coli gamma-aminobutyrate aminotransferase (see paper)
30% identity, 94% coverage: 24:437/442 of query aligns to 2:422/425 of 1sf2A
- active site: V18 (= V40), Y137 (= Y156), E205 (≠ D223), D238 (= D256), Q241 (= Q259), K267 (= K286), T296 (= T316), R397 (≠ K416)
- binding pyridoxal-5'-phosphate: G110 (= G129), S111 (≠ T130), Y137 (= Y156), H138 (= H157), E205 (≠ D223), D238 (= D256), V240 (= V258), Q241 (= Q259), K267 (= K286)
- binding sulfate ion: N152 (≠ G171), Y393 (≠ G412)
3q8nC Crystal structure of 4-aminobutyrate transaminase from mycobacterium smegmatis (see paper)
33% identity, 92% coverage: 23:429/442 of query aligns to 15:425/439 of 3q8nC
- active site: V32 (= V40), Y151 (= Y156), E221 (≠ D223), D254 (= D256), Q257 (= Q259), K283 (= K286), T312 (= T316), R412 (≠ K416)
- binding 4-oxobutanoic acid: G124 (= G129), A125 (≠ T130), V256 (= V258), K283 (= K286)
P22256 4-aminobutyrate aminotransferase GabT; 5-aminovalerate transaminase; GABA aminotransferase; GABA-AT; Gamma-amino-N-butyrate transaminase; GABA transaminase; Glutamate:succinic semialdehyde transaminase; L-AIBAT; EC 2.6.1.19; EC 2.6.1.48 from Escherichia coli (strain K12) (see 2 papers)
30% identity, 94% coverage: 24:437/442 of query aligns to 3:423/426 of P22256
- I50 (≠ V73) mutation to Q: 3-fold decrease in catalytic activity and 12-fold decrease in affinity for GABA.
- GS 111:112 (≠ GT 129:130) binding
- E211 (≠ S228) mutation to S: 100-fold decrease in catalytic activity and 15-fold decrease in affinity for GABA.
- V241 (= V258) mutation to A: 25-fold decrease in catalytic activity and 5-fold decrease in affinity for GABA.
- Q242 (= Q259) binding
- K268 (= K286) modified: N6-(pyridoxal phosphate)lysine
- T297 (= T316) binding
7vo1A Structure of aminotransferase-substrate complex (see paper)
32% identity, 95% coverage: 13:430/442 of query aligns to 1:431/452 of 7vo1A
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid: I61 (vs. gap), S121 (= S128), G122 (= G129), T123 (= T130), F149 (≠ Y156), H150 (= H157), R152 (≠ H159), E234 (≠ S228), D262 (= D256), V264 (= V258), Q265 (= Q259), K291 (= K286), N318 (= N315), T319 (= T316), R417 (≠ K416)
7vntA Structure of aminotransferase-substrate complex (see paper)
32% identity, 95% coverage: 13:430/442 of query aligns to 1:431/452 of 7vntA
- binding L-ornithine: F149 (≠ Y156), R152 (≠ H159), E234 (≠ S228), K291 (= K286)
- binding pyridoxal-5'-phosphate: G122 (= G129), T123 (= T130), F149 (≠ Y156), H150 (= H157), E229 (≠ D223), D262 (= D256), V264 (= V258), Q265 (= Q259), K291 (= K286)
7vnoA Structure of aminotransferase (see paper)
32% identity, 95% coverage: 13:430/442 of query aligns to 1:431/452 of 7vnoA
O50131 Ornithine aminotransferase; Orn-AT; Ornithine delta-aminotransferase; EC 2.6.1.13 from Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) (see paper)
32% identity, 95% coverage: 13:430/442 of query aligns to 3:433/454 of O50131
- T92 (= T98) mutation to V: Slightly increases the specific activity. Increases KM for L-ornithine.
- D93 (≠ R99) mutation to L: Reduces the specific activity. Increases KM for L-ornithine.
- G124 (= G129) binding
- T125 (= T130) binding
- Q267 (= Q259) binding
- K293 (= K286) modified: N6-(pyridoxal phosphate)lysine
- T321 (= T316) binding
A0QYS9 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
31% identity, 89% coverage: 47:439/442 of query aligns to 19:383/390 of A0QYS9
- K304 (≠ A348) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
O58478 Alanine/serine racemase; ASR; Ala/Ser racemase; EC 5.1.1.-; EC 5.1.1.1 from Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) (see paper)
29% identity, 94% coverage: 23:439/442 of query aligns to 30:462/474 of O58478
- D251 (≠ S228) mutation to A: Loss of activity.
- K308 (= K286) mutation to A: Loss of activity.
Query Sequence
>HSERO_RS00035 FitnessBrowser__HerbieS:HSERO_RS00035
MTHADGMLALNAFNPQSGSTTAPATRALIERRRNTFGDGVPLFYRDPVHFVSASGVWLRD
QDGLEYLDAYNNVPSVGHCHPRVVEAVSKQAATLNTHTRYLSDVVTSYAERLLGTLPREL
SKVLFTSSGTESVDLAMRLARLYTGGSGFIVTRFAYHGHSTAVAEITPAFGPGVPIGINV
RLVDAPDGYRQDAPVGIKFAQDVAAAIADMERHGIRFAGLILDTVCSSDGLFVDPPGFLK
DAIATVKKAGGVFIADEVQPGFGRTGEGMWGFERHRIVPDIVVMGKPMGNGMPIAATVTR
ADIMQAFTERSGYFNTFGGNTVCCAAASAVLDVIESEGLINNAKETGASLKLGLEQLKGQ
HQCIGDVRAIGLYAAVEFVLPDTKTADTDMALHVVNTLRQKRILISTCGPAGNILKIRPP
LQFSRQHCDLLVTAIDDVLHMR
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory