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PDXA_PSEA6
ID   PDXA_PSEA6              Reviewed;         326 AA.
AC   Q15QB2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=4-hydroxythreonine-4-phosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00536};
DE            EC=1.1.1.262 {ECO:0000255|HAMAP-Rule:MF_00536};
DE   AltName: Full=4-(phosphohydroxy)-L-threonine dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00536};
GN   Name=pdxA {ECO:0000255|HAMAP-Rule:MF_00536}; OrderedLocusNames=Patl_3420;
OS   Pseudoalteromonas atlantica (strain T6c / ATCC BAA-1087).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=342610;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T6c / ATCC BAA-1087;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Karls A.C.,
RA   Bartlett D., Higgins B.P., Richardson P.;
RT   "Complete sequence of Pseudoalteromonas atlantica T6c.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-
CC       threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which
CC       spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate
CC       (AHAP). {ECO:0000255|HAMAP-Rule:MF_00536}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-(phosphooxy)-L-threonine + NAD(+) = 3-amino-2-oxopropyl
CC         phosphate + CO2 + NADH; Xref=Rhea:RHEA:32275, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57279, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:58452; EC=1.1.1.262; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00536};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00536};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00536};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00536};
CC       Note=Binds 1 divalent metal cation per subunit. Can use ions such as
CC       Zn(2+), Mg(2+) or Co(2+). {ECO:0000255|HAMAP-Rule:MF_00536};
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis;
CC       pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 4/5.
CC       {ECO:0000255|HAMAP-Rule:MF_00536}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00536}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00536}.
CC   -!- MISCELLANEOUS: The active site is located at the dimer interface.
CC       {ECO:0000255|HAMAP-Rule:MF_00536}.
CC   -!- SIMILARITY: Belongs to the PdxA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00536}.
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DR   EMBL; CP000388; ABG41926.1; -; Genomic_DNA.
DR   RefSeq; WP_011576155.1; NC_008228.1.
DR   AlphaFoldDB; Q15QB2; -.
DR   SMR; Q15QB2; -.
DR   STRING; 342610.Patl_3420; -.
DR   EnsemblBacteria; ABG41926; ABG41926; Patl_3420.
DR   KEGG; pat:Patl_3420; -.
DR   eggNOG; COG1995; Bacteria.
DR   HOGENOM; CLU_040168_1_0_6; -.
DR   OMA; TAQVVMM; -.
DR   OrthoDB; 1414545at2; -.
DR   UniPathway; UPA00244; UER00312.
DR   Proteomes; UP000001981; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050570; F:4-hydroxythreonine-4-phosphate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0050897; F:cobalt ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00536; PdxA; 1.
DR   InterPro; IPR037510; PdxA.
DR   InterPro; IPR005255; PdxA_fam.
DR   PANTHER; PTHR30004; PTHR30004; 1.
DR   Pfam; PF04166; PdxA; 1.
DR   TIGRFAMs; TIGR00557; pdxA; 1.
PE   3: Inferred from homology;
KW   Cobalt; Cytoplasm; Magnesium; Metal-binding; NAD; NADP; Oxidoreductase;
KW   Pyridoxine biosynthesis; Reference proteome; Zinc.
FT   CHAIN           1..326
FT                   /note="4-hydroxythreonine-4-phosphate dehydrogenase"
FT                   /id="PRO_1000128257"
FT   BINDING         133
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00536"
FT   BINDING         134
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00536"
FT   BINDING         163
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00536"
FT   BINDING         208
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00536"
FT   BINDING         263
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00536"
FT   BINDING         271
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00536"
FT   BINDING         280
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00536"
FT   BINDING         289
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00536"
SQ   SEQUENCE   326 AA;  35063 MW;  65BD0237F78722A7 CRC64;
     MTIKLAITPG EPAGVGPDLI ITLAQQQWQA MLVVFANAEL MRTRANELNI PLTLLPYDAS
     RTDIQPAGSL YIVDIPLQDE VIAGKLNPTN SQYVLDTLHQ ACQMNLNGEF QALVTGPVHK
     GVINEAGIPF SGHTEFFAQQ SNTPEVVMML ATEGLRVTLA TTHIPVTAVS AAITQPKLDN
     VIRIIDHDLR TKFGIAKPHI FVCGLNPHAG EDGHIGREEI DTIIPALNAL RQEGITLTGP
     LPADTIFNPK YLQQADTVLA MYHDQGLPVL KYKGFSQAVN ITLGLPFIRT SVDHGTALDL
     AATGQADVGS FSIAIKEAIS LAKSTQ
 
 
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