(data stored in ACNUC7421 zone)

SWISSPROT: PDXA_SALTY

ID   PDXA_SALTY              Reviewed;         329 AA.
AC   P58717;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   31-JAN-2002, sequence version 1.
DT   11-DEC-2019, 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=STM0091;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH COBALT IONS,
RP   COFACTOR, AND SUBUNIT.
RG   Midwest center for structural genomics (MCSG);
RT   "Crystal structure of NAD-dependent dehydrogenase/carboxylase of Salmonella
RT   typhimurium.";
RL   Submitted (JAN-2005) to the PDB data bank.
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, ECO:0000269|Ref.2};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00536, ECO:0000269|Ref.2};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00536, ECO:0000269|Ref.2};
CC       Note=Binds 1 divalent metal cation per subunit. Can probably use ions
CC       such as Zn(2+), Mg(2+) or Co(2+). {ECO:0000255|HAMAP-Rule:MF_00536,
CC       ECO:0000269|Ref.2};
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       ECO:0000269|Ref.2}.
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}.
DR   EMBL; AE006468; AAL19055.1; -; Genomic_DNA.
DR   RefSeq; NP_459096.1; NC_003197.2.
DR   RefSeq; WP_000093016.1; NC_003197.2.
DR   PDB; 1R8K; X-ray; 2.10 A; A/B=1-329.
DR   PDBsum; 1R8K; -.
DR   SMR; P58717; -.
DR   PaxDb; P58717; -.
DR   PRIDE; P58717; -.
DR   EnsemblBacteria; AAL19055; AAL19055; STM0091.
DR   GeneID; 1251609; -.
DR   KEGG; stm:STM0091; -.
DR   PATRIC; fig|99287.12.peg.94; -.
DR   eggNOG; ENOG4105CEZ; Bacteria.
DR   eggNOG; COG1995; LUCA.
DR   HOGENOM; HOG000221592; -.
DR   KO; K00097; -.
DR   OMA; HKGVINE; -.
DR   PhylomeDB; P58717; -.
DR   BioCyc; SENT99287:STM0091-MONOMER; -.
DR   UniPathway; UPA00244; UER00312.
DR   EvolutionaryTrace; P58717; -.
DR   Proteomes; UP000001014; 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   1: Evidence at protein level;
DR   PRODOM; P58717.
DR   SWISS-2DPAGE; P58717.
KW   3D-structure; Cobalt; Cytoplasm; Magnesium; Metal-binding; NAD; NADP;
KW   Oxidoreductase; Pyridoxine biosynthesis; Reference proteome; Zinc.
FT   CHAIN           1..329
FT                   /note="4-hydroxythreonine-4-phosphate dehydrogenase"
FT                   /id="PRO_0000188826"
FT   METAL           166
FT                   /note="Divalent metal cation; shared with dimeric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00536,
FT                   ECO:0000305|Ref.2"
FT   METAL           211
FT                   /note="Divalent metal cation; shared with dimeric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00536,
FT                   ECO:0000305|Ref.2"
FT   METAL           266
FT                   /note="Divalent metal cation; shared with dimeric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00536,
FT                   ECO:0000305|Ref.2"
FT   BINDING         136
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00536"
FT   BINDING         137
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00536"
FT   BINDING         274
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00536"
FT   BINDING         283
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00536"
FT   BINDING         292
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00536"
FT   STRAND          6..10
FT                   /evidence="ECO:0000244|PDB:1R8K"
FT   HELIX           18..25
FT                   /evidence="ECO:0000244|PDB:1R8K"
FT   STRAND          31..38
FT                   /evidence="ECO:0000244|PDB:1R8K"
FT   HELIX           40..49
FT                   /evidence="ECO:0000244|PDB:1R8K"
FT   STRAND          55..58
FT                   /evidence="ECO:0000244|PDB:1R8K"
FT   STRAND          72..77
FT                   /evidence="ECO:0000244|PDB:1R8K"
FT   HELIX           91..93
FT                   /evidence="ECO:0000244|PDB:1R8K"
FT   HELIX           94..109
FT                   /evidence="ECO:0000244|PDB:1R8K"
FT   STRAND          114..118
FT                   /evidence="ECO:0000244|PDB:1R8K"
FT   HELIX           123..127
FT                   /evidence="ECO:0000244|PDB:1R8K"
FT   TURN            128..130
FT                   /evidence="ECO:0000244|PDB:1R8K"
FT   HELIX           136..143
FT                   /evidence="ECO:0000244|PDB:1R8K"
FT   STRAND          150..154
FT                   /evidence="ECO:0000244|PDB:1R8K"
FT   STRAND          159..164
FT                   /evidence="ECO:0000244|PDB:1R8K"
FT   HELIX           169..171
FT                   /evidence="ECO:0000244|PDB:1R8K"
FT   HELIX           172..175
FT                   /evidence="ECO:0000244|PDB:1R8K"
FT   HELIX           178..194
FT                   /evidence="ECO:0000244|PDB:1R8K"
FT   STRAND          202..206
FT                   /evidence="ECO:0000244|PDB:1R8K"
FT   HELIX           210..216
FT                   /evidence="ECO:0000244|PDB:1R8K"
FT   HELIX           221..224
FT                   /evidence="ECO:0000244|PDB:1R8K"
FT   HELIX           226..234
FT                   /evidence="ECO:0000244|PDB:1R8K"
FT   TURN            235..237
FT                   /evidence="ECO:0000244|PDB:1R8K"
FT   STRAND          239..244
FT                   /evidence="ECO:0000244|PDB:1R8K"
FT   HELIX           246..249
FT                   /evidence="ECO:0000244|PDB:1R8K"
FT   HELIX           252..255
FT                   /evidence="ECO:0000244|PDB:1R8K"
FT   STRAND          259..265
FT                   /evidence="ECO:0000244|PDB:1R8K"
FT   HELIX           266..277
FT                   /evidence="ECO:0000244|PDB:1R8K"
FT   STRAND          282..290
FT                   /evidence="ECO:0000244|PDB:1R8K"
FT   STRAND          292..294
FT                   /evidence="ECO:0000244|PDB:1R8K"
FT   TURN            301..306
FT                   /evidence="ECO:0000244|PDB:1R8K"
FT   HELIX           312..327
FT                   /evidence="ECO:0000244|PDB:1R8K"
SQ   SEQUENCE   329 AA;  34779 MW;  054D9F4E0F34E43B CRC64;
     MSSAQRVVIT PGEPAGSGPD LVVQLAQRAW PIELVVCADG ALLTERAAML GLPLSLLPYS
     PDVPAAPQPA GTLTLLPVSL RAPAISGQLT VENGPYVVET LARACDGCLN GEFAALITGP
     VHKGVINDAG ISFTGHTEFF EERSQAKKVV MMLATEELRV ALATTHLPLR AIADAITPAL
     LHEVIAILHH DLRTKFGIAE PRILVCGLNP HAGEGGHMGT EEIDTIIPVL DELRAQGMKL
     NGPLPADTLF QPKYLDNADA VLAMYHDQGL PVLKYQGFGR GVNITLGLPF IRTSVDHGTA
     LELAGRGKAD VGSFITALNL AIKMIVNTQ
//

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