(data stored in SCRATCH zone)

SWISSPROT: A0A0H2ZLL0_PSEAB

ID   A0A0H2ZLL0_PSEAB        Unreviewed;       328 AA.
AC   A0A0H2ZLL0;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   07-JUN-2017, entry version 13.
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   ECO:0000313|EMBL:ABJ15557.1};
GN   OrderedLocusNames=PA14_07740 {ECO:0000313|EMBL:ABJ15557.1};
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963 {ECO:0000313|EMBL:ABJ15557.1, ECO:0000313|Proteomes:UP000000653};
RN   [1] {ECO:0000313|EMBL:ABJ15557.1, ECO:0000313|Proteomes:UP000000653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14 {ECO:0000313|EMBL:ABJ15557.1,
RC   ECO:0000313|Proteomes:UP000000653};
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
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; CP000438; ABJ15557.1; -; Genomic_DNA.
DR   RefSeq; WP_003137368.1; NC_008463.1.
DR   ProteinModelPortal; A0A0H2ZLL0; -.
DR   EnsemblBacteria; ABJ15557; ABJ15557; PA14_07740.
DR   KEGG; pau:PA14_07740; -.
DR   KO; K00097; -.
DR   OMA; APVHKGV; -.
DR   UniPathway; UPA00244; UER00312.
DR   Proteomes; UP000000653; 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; A0A0H2ZLL0.
DR   SWISS-2DPAGE; A0A0H2ZLL0.
KW   Cobalt {ECO:0000256|HAMAP-Rule:MF_00536};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000653};
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};
KW   Pyridoxine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00536};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00536}.
FT   METAL       165    165       Divalent metal cation; shared with
FT                                dimeric partner. {ECO:0000256|HAMAP-Rule:
FT                                MF_00536}.
FT   METAL       210    210       Divalent metal cation; shared with
FT                                dimeric partner. {ECO:0000256|HAMAP-Rule:
FT                                MF_00536}.
FT   METAL       265    265       Divalent metal cation; shared with
FT                                dimeric partner. {ECO:0000256|HAMAP-Rule:
FT                                MF_00536}.
FT   BINDING     135    135       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00536}.
FT   BINDING     136    136       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00536}.
FT   BINDING     273    273       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00536}.
FT   BINDING     282    282       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00536}.
FT   BINDING     291    291       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00536}.
SQ   SEQUENCE   328 AA;  34941 MW;  23B1C67796CD8A35 CRC64;
     MSLRFALTPG EPAGIGPDLC LLLARSAQPH PLIAIASRTL LQERAGQLGL AIYLKDVSPA
     AWPERPAKAG QLYVWDTPLA APVRPGQLDR ANAAYVLETL TRAGQGCLDG HFAGMITAPV
     HKGVINEAGI PFSGHTEFLA DLTHTAQVVM MLATRGLRVA LATTHLPLRE VADAISDERL
     ARVARILHAD LRDKFGIAHP RILVCGLNPH AGEGGHLGRE EIEVIEPCLE RLRGEGLDLI
     GPLPADTLFT PKHLEHCDAV LAMYHDQGLP VLKYKGFGAA VNVTLGLPII RTSVDHGTAL
     DLAGSGRIDS GSLQVALETA YQMAASRC
//

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