SitesBLAST

Q8L940 Pyridoxal 5'-phosphate synthase subunit PDX1.3; AtPDX1.3; AtPDX1;1; PLP synthase subunit PDX1.3; EC 4.3.3.6 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
38% identity, 23% coverage: 183:243/268 of query aligns to 208:271/309 of Q8L940

query
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Q8L940

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Sites not aligning to the query:

54 G→S: In rsr4-1; strongly reduced oligomerization and 63% reduction in pyridoxal biosynthesis.

5lnuA Crystal structure of arabidopsis thaliana pdx1-i320 complex (see paper)
27% identity, 59% coverage: 85:243/268 of query aligns to 119:251/277 of 5lnuA

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binding (4~{S})-4-azanyl-5-oxidanyl-pent-1-en-3-one: R143 (≠ K114), K145 (≠ E116)
binding phosphate ion: G149 (≠ D120), G209 (vs. gap), G210 (= G202), G231 (≠ S223), S232 (≠ T224)

Sites not aligning to the query:

5k2zB Pdx1.3-adduct (arabidopsis) (see paper)
38% identity, 23% coverage: 183:243/268 of query aligns to 189:252/278 of 5k2zB

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5k2zB

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Sites not aligning to the query:

binding 2-azanylpenta-1,4-dien-3-one: 21, 78, 144, 146

5lnrA Crystal structure of arabidopsis thaliana pdx1-plp complex (see paper)
38% identity, 23% coverage: 183:243/268 of query aligns to 188:251/267 of 5lnrA

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Sites not aligning to the query:

binding pyridoxal-5'-phosphate: 111, 126, 130, 133, 134, 145

Q9WYU4 Pyridoxal 5'-phosphate synthase subunit PdxS; PLP synthase subunit PdxS; Pdx1; EC 4.3.3.6 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) (see paper)
48% identity, 16% coverage: 202:243/268 of query aligns to 215:256/293 of Q9WYU4

query
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Q9WYU4

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G215 (= G202) binding D-ribose 5-phosphate
GS 236:237 (≠ ST 223:224) binding D-ribose 5-phosphate

Sites not aligning to the query:

25 binding D-ribose 5-phosphate
82 active site, Schiff-base intermediate with D-ribose 5-phosphate
103 binding D-ribulose 5-phosphate
154 binding D-ribose 5-phosphate

5lntA Crystal structure of arabidopsis thaliana pdx1k166r-prei320 complex (see paper)
37% identity, 25% coverage: 180:247/268 of query aligns to 186:256/273 of 5lntA

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binding [(~{E},4~{S})-4-azanyl-3-oxidanylidene-pent-1-enyl] dihydrogen phosphate: G210 (vs. gap), G211 (= G202), F230 (≠ L221), G232 (≠ S223), S233 (≠ T224)

Sites not aligning to the query:

binding [(~{E},4~{S})-4-azanyl-3-oxidanylidene-pent-1-enyl] dihydrogen phosphate: 21, 46, 78, 99, 149, 150

2issB Structure of the plp synthase holoenzyme from thermotoga maritima (see paper)
48% identity, 16% coverage: 202:243/268 of query aligns to 220:261/285 of 2issB

query
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2issB

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binding ribulose-5-phosphate: G220 (= G202), G241 (≠ S223), S242 (≠ T224)

Sites not aligning to the query:

binding ribulose-5-phosphate: 30, 55, 87, 108, 153, 158, 159, 219

Q03148 Pyridoxal 5'-phosphate synthase subunit SNZ1; PLP synthase subunit SNZ1; PDX1 homolog 1; Pdx1.1; p35; EC 4.3.3.6 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
36% identity, 20% coverage: 189:242/268 of query aligns to 199:254/297 of Q03148

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Q03148

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K240 (≠ R228) mutation to A: No effect.

Sites not aligning to the query:

116 E→A: No effect.
117 K→A: No activity.
136:137 RR→AA: No pyridoxal 5'-phosphate synthesis activity. Retains ability to isomerize dihydroxyacetone phosphate to glyceraldehyde 3-phosphate.
148 K→A: No activity.
164 binding D-glyceraldehyde 3-phosphate; R→A: No pyridoxal 5'-phosphate synthesis activity. Retains ability to isomerize dihydroxyacetone phosphate to glyceraldehyde 3-phosphate.

3o05A Crystal structure of yeast pyridoxal 5-phosphate synthase snz1 complxed with substrate plp (see paper)
36% identity, 20% coverage: 189:242/268 of query aligns to 185:240/261 of 3o05A

query
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3o05A

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Sites not aligning to the query:

binding pyridoxal-5'-phosphate: 97, 122, 123, 134

Query Sequence

>WP_005459628.1 NCBI__GCF_000244975.1:WP_005459628.1
MSTSTGSDVRAAVAGEDGGDQLVINDHKLTSRLIIGTGGASNLSVLERALVASGTELTTV
AMRRADTEGGSGVLDLLRRLGIELLPNTAGCRNAAEAVLTAQLAREALGTDLVKLEVHAD
DRTLLPDPVETLEAAERLVADGFTVLAYTNDDPVLALRLEEAGCAAVMPLGSPIGTGLGI
RNPHNIELIVSRAGVPIILDAGIGTASDAALAMELGCDGVLLSTAVTRAQDPERMAHAMR
SAVLAGRLARQAGRIPRRFWAQASSPPR

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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