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4-hydroxythreonine-4-phosphate dehydrogenase (EC 1.1.1.262) (4-(phosphohydroxy)-L-threonine dehydrogenase)

 A8QM16_9BACT            Unreviewed;       367 AA.
A8QM16;
15-JAN-2008, integrated into UniProtKB/TrEMBL.
15-JAN-2008, sequence version 1.
27-SEP-2017, entry version 47.
RecName: Full=4-hydroxythreonine-4-phosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00536};
EC=1.1.1.262 {ECO:0000256|HAMAP-Rule:MF_00536};
AltName: Full=4-(phosphohydroxy)-L-threonine dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00536};
Name=pdxA {ECO:0000256|HAMAP-Rule:MF_00536};
ORFNames=HOT0_02H05.0003 {ECO:0000313|EMBL:ABL97500.1};
uncultured marine bacterium HOT0_02H05.
Bacteria; environmental samples.
NCBI_TaxID=415450 {ECO:0000313|EMBL:ABL97500.1};
[1] {ECO:0000313|EMBL:ABL97500.1}
NUCLEOTIDE SEQUENCE.
PubMed=17971441; DOI=10.1073/pnas.0701017104;
Zehr J.P., Bench S.R., Mondragon E.A., McCarren J., DeLong E.F.;
"Low genomic diversity in tropical oceanic N2-fixing cyanobacteria.";
Proc. Natl. Acad. Sci. U.S.A. 104:17807-17812(2007).
-!- FUNCTION: Catalyzes the NAD(P)-dependent oxidation of 4-
(phosphohydroxy)-L-threonine (HTP) into 2-amino-3-oxo-4-
(phosphohydroxy)butyric acid which spontaneously decarboxylates to
form 3-amino-2-oxopropyl phosphate (AHAP). {ECO:0000256|HAMAP-
Rule:MF_00536}.
-!- CATALYTIC ACTIVITY: 4-phosphonooxy-L-threonine + NAD(+) = 3-amino-
2-oxopropyl phosphate + CO(2) + NADH. {ECO:0000256|HAMAP-
Rule:MF_00536}.
-!- COFACTOR:
Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
Evidence={ECO:0000256|HAMAP-Rule:MF_00536};
Note=Binds 1 divalent metal cation per subunit.
{ECO:0000256|HAMAP-Rule:MF_00536};
-!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate
biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-
phosphate: step 4/5. {ECO:0000256|HAMAP-Rule:MF_00536}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00536,
ECO:0000256|SAAS:SAAS00701244}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00536}.
-!- MISCELLANEOUS: The active site is located at the dimer interface.
{ECO:0000256|HAMAP-Rule:MF_00536}.
-!- SIMILARITY: Belongs to the PdxA family. {ECO:0000256|HAMAP-
Rule:MF_00536, ECO:0000256|SAAS:SAAS00701249}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00536}.
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EMBL; EF089389; ABL97500.1; -; Genomic_DNA.
ProteinModelPortal; A8QM16; -.
UniPathway; UPA00244; UER00312.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0050570; F:4-hydroxythreonine-4-phosphate dehydrogenase activity; IEA:UniProtKB-UniRule.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
GO; GO:0051287; F:NAD binding; IEA:InterPro.
GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-UniRule.
HAMAP; MF_00536; PdxA; 1.
InterPro; IPR005255; PdxA.
PANTHER; PTHR30004; PTHR30004; 1.
Pfam; PF04166; PdxA; 1.
TIGRFAMs; TIGR00557; pdxA; 1.
3: Inferred from homology;
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00536};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00536,
ECO:0000256|SAAS:SAAS00701256};
NAD {ECO:0000256|HAMAP-Rule:MF_00536, ECO:0000256|SAAS:SAAS00701266};
NADP {ECO:0000256|HAMAP-Rule:MF_00536};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00536,
ECO:0000256|SAAS:SAAS00701261};
Pyridoxine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00536}.
METAL 176 176 Divalent metal cation; shared with
dimeric partner. {ECO:0000256|HAMAP-
Rule:MF_00536}.
METAL 221 221 Divalent metal cation; shared with
dimeric partner. {ECO:0000256|HAMAP-
Rule:MF_00536}.
METAL 303 303 Divalent metal cation; shared with
dimeric partner. {ECO:0000256|HAMAP-
Rule:MF_00536}.
BINDING 141 141 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00536}.
BINDING 311 311 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00536}.
BINDING 320 320 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00536}.
BINDING 329 329 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00536}.
SEQUENCE 367 AA; 40205 MW; CA00FE0BF11B479F CRC64;
MQFSDSPQRQ RPHLALTMGD PASIGPEIIL KALADPTISE TCDLTVIGTR SLLEKTYQEL
HLQGQPLVHP DNLSIIDIPL DPNTIEQIMP GSGNGASGKA SFLYLETAIA HTLEGKFQGI
VTAPIAKSCW KAAGYSYPGQ TEVLAQKAKI ERFGMLFVGR SPYTGWTLRT LLATTHIPLN
HVSQTLTPQL MSLKLDLLIN CLQQDFAIEN PKIVISGLNP HSGENGQLGT EEKDWLFPWL
EKAQQQYSHA EIVGLVPPDT LWVNPAKAWY GDTLKITQTG DTARDRPTLT LNNVGDAYLA
LYHDQGLIPV KLMAFDQAIN TTIGLPFIRT SPDHGTAFDI AGKGIARETS LKAAIELAVE
LTKQRLR


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