(data stored in ACNUC7421 zone)

SWISSPROT: C5B7P2_EDWI9

ID   C5B7P2_EDWI9            Unreviewed;       331 AA.
AC   C5B7P2;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 59.
DE   RecName: Full=4-hydroxythreonine-4-phosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00536};
DE            EC=1.1.1.262 {ECO:0000256|HAMAP-Rule:MF_00536};
DE   AltName: Full=4-(phosphohydroxy)-L-threonine dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00536};
GN   Name=pdxA {ECO:0000256|HAMAP-Rule:MF_00536};
GN   OrderedLocusNames=NT01EI_0697 {ECO:0000313|EMBL:ACR67919.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67919.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the NAD(P)-dependent oxidation of 4-
CC       (phosphohydroxy)-L-threonine (HTP) into 2-amino-3-oxo-4-
CC       (phosphohydroxy)butyric acid which spontaneously decarboxylates to
CC       form 3-amino-2-oxopropyl phosphate (AHAP). {ECO:0000256|HAMAP-
CC       Rule:MF_00536}.
CC   -!- CATALYTIC ACTIVITY: 4-phosphonooxy-L-threonine + NAD(+) = 3-amino-
CC       2-oxopropyl phosphate + CO(2) + NADH. {ECO:0000256|HAMAP-
CC       Rule:MF_00536}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00536};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00536};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00536};
CC       Note=Binds 1 divalent metal cation per subunit. Can use ions such
CC       as Zn(2+), Mg(2+) or Co(2+). {ECO:0000256|HAMAP-Rule:MF_00536};
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate
CC       biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-
CC       phosphate: step 4/5. {ECO:0000256|HAMAP-Rule:MF_00536}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00536,
CC       ECO:0000256|SAAS:SAAS00701244}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00536}.
CC   -!- MISCELLANEOUS: The active site is located at the dimer interface.
CC       {ECO:0000256|HAMAP-Rule:MF_00536}.
CC   -!- SIMILARITY: Belongs to the PdxA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00536, ECO:0000256|SAAS:SAAS00701249}.
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DR   EMBL; CP001600; ACR67919.1; -; Genomic_DNA.
DR   RefSeq; WP_015870112.1; NC_012779.2.
DR   ProteinModelPortal; C5B7P2; -.
DR   STRING; 634503.NT01EI_0697; -.
DR   EnsemblBacteria; ACR67919; ACR67919; NT01EI_0697.
DR   GeneID; 7962031; -.
DR   KEGG; eic:NT01EI_0697; -.
DR   PATRIC; fig|634503.3.peg.628; -.
DR   eggNOG; ENOG4105CEZ; Bacteria.
DR   eggNOG; COG1995; LUCA.
DR   HOGENOM; HOG000221592; -.
DR   KO; K00097; -.
DR   OMA; APVHKGV; -.
DR   OrthoDB; POG091H03XD; -.
DR   UniPathway; UPA00244; UER00312.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050570; F:4-hydroxythreonine-4-phosphate dehydrogenase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0050897; F:cobalt ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_00536; PdxA; 1.
DR   InterPro; IPR005255; PdxA.
DR   PANTHER; PTHR30004; PTHR30004; 1.
DR   Pfam; PF04166; PdxA; 1.
DR   TIGRFAMs; TIGR00557; pdxA; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5B7P2.
DR   SWISS-2DPAGE; C5B7P2.
KW   Cobalt {ECO:0000256|HAMAP-Rule:MF_00536};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00536};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00536};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00536,
KW   ECO:0000256|SAAS:SAAS00701256};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00536, ECO:0000256|SAAS:SAAS00701266};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00536};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00536,
KW   ECO:0000256|SAAS:SAAS00701261, ECO:0000313|EMBL:ACR67919.1};
KW   Pyridoxine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00536};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00536}.
FT   METAL       166    166       Divalent metal cation; shared with
FT                                dimeric partner. {ECO:0000256|HAMAP-Rule:
FT                                MF_00536}.
FT   METAL       211    211       Divalent metal cation; shared with
FT                                dimeric partner. {ECO:0000256|HAMAP-Rule:
FT                                MF_00536}.
FT   METAL       266    266       Divalent metal cation; shared with
FT                                dimeric partner. {ECO:0000256|HAMAP-Rule:
FT                                MF_00536}.
FT   BINDING     136    136       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00536}.
FT   BINDING     137    137       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00536}.
FT   BINDING     274    274       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00536}.
FT   BINDING     283    283       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00536}.
FT   BINDING     292    292       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00536}.
SQ   SEQUENCE   331 AA;  35272 MW;  433D5E65C275F4D9 CRC64;
     MASIRRIVIT PGEPAGVGPE LLVQLAQRPW PAELVVCADP GLLEARAHAL GLPLTLRRYD
     SALSPQAQQA ATLTVLPIPL EADVIPGKLN VANGNYVVAT LTRACDGCLS GEFAALVTGP
     VHKGIINDAG VPFTGHTEFF ADRSGCPRVV MMLASERLRV ALATTHLPLQ EVPAAITPQT
     LREVITILDA DLRRRFGLRQ PHIYVCGLNP HAGEGGHMGR EELDIIIPTL DALRASAIHL
     TGPLPADTLF QAKYLDDADA VLAMYHDQGL PVLKYQGFGR AVNITLGLPF IRTSVDHGTA
     LDLAASGQAQ PGSFITALNL AIEMTNHSNE Q
//

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