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Database: UniProt
Entry: I1XKV7_METNJ
LinkDB: I1XKV7_METNJ
Original site: I1XKV7_METNJ 
ID   I1XKV7_METNJ            Unreviewed;       331 AA.
AC   I1XKV7;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   24-JAN-2024, entry version 60.
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=Q7A_2214 {ECO:0000313|EMBL:AFI85026.1};
OS   Methylophaga nitratireducenticrescens.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Methylophaga.
OX   NCBI_TaxID=754476 {ECO:0000313|EMBL:AFI85026.1, ECO:0000313|Proteomes:UP000009144};
RN   [1] {ECO:0000313|EMBL:AFI85026.1, ECO:0000313|Proteomes:UP000009144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JAM1 {ECO:0000313|EMBL:AFI85026.1,
RC   ECO:0000313|Proteomes:UP000009144};
RX   PubMed=22815445; DOI=10.1128/JB.00726-12;
RA   Villeneuve C., Martineau C., Mauffrey F., Villemur R.;
RT   "Complete genome sequences of Methylophaga sp. strain JAM1 and Methylophaga
RT   sp. strain JAM7.";
RL   J. Bacteriol. 194:4126-4127(2012).
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:0000256|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:0000256|HAMAP-
CC         Rule:MF_00536};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00536};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00536};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00536}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00536}.
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}.
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DR   EMBL; CP003390; AFI85026.1; -; Genomic_DNA.
DR   RefSeq; WP_014707394.1; NC_017857.3.
DR   AlphaFoldDB; I1XKV7; -.
DR   STRING; 754476.Q7A_2214; -.
DR   KEGG; mej:Q7A_2214; -.
DR   PATRIC; fig|754476.3.peg.2189; -.
DR   eggNOG; COG1995; Bacteria.
DR   HOGENOM; CLU_040168_1_0_6; -.
DR   OMA; TAQVVMM; -.
DR   OrthoDB; 9801783at2; -.
DR   UniPathway; UPA00244; UER00312.
DR   Proteomes; UP000009144; 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   Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR   HAMAP; MF_00536; PdxA; 1.
DR   InterPro; IPR037510; PdxA.
DR   InterPro; IPR005255; PdxA_fam.
DR   NCBIfam; TIGR00557; pdxA; 1.
DR   PANTHER; PTHR30004; 4-HYDROXYTHREONINE-4-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR30004:SF5; 4-HYDROXYTHREONINE-4-PHOSPHATE DEHYDROGENASE; 1.
DR   Pfam; PF04166; PdxA; 1.
DR   SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
PE   3: Inferred from homology;
KW   Cobalt {ECO:0000256|HAMAP-Rule:MF_00536};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00536};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00536};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00536}; NAD {ECO:0000256|HAMAP-Rule:MF_00536};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00536};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00536}; Pyridoxine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00536};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00536}.
FT   BINDING         136
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00536"
FT   BINDING         137
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00536"
FT   BINDING         166
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00536"
FT   BINDING         211
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00536"
FT   BINDING         266
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00536"
FT   BINDING         274
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00536"
FT   BINDING         283
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00536"
FT   BINDING         292
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00536"
SQ   SEQUENCE   331 AA;  35300 MW;  63A4AFA79F63D754 CRC64;
     MSDICRIALT SGEPAGIGPD LCIQLAQQGQ RHEIVVIADP ELLQQRADEL SLPLKLVEFD
     PNSDPKPGEA GRIVYLASKL AEKVVPGKLN PANSAYVIDT LQLALNGCLD GTFDAVVTAP
     VHKGVINDAQ IPFSGHTEFF ADGAGVNKVV MMLATPELRV ALATTHLPLR EVSDAVTQQS
     LLQIMRILAN GLHFSFGLKH PRIAVCGLNP HAGEGGHLGA EEQTVIEPAI KLIREQGYEF
     NGPWPADTIF VKSRLAEYDA VLAMYHDQGL PVLKHQGFGD AVNITLGLPF IRTSVDHGTA
     LDLAASGNAS ATSLQAAINM AETMSLSRRT A
//
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