ID N1ZP05_9CLOT Unreviewed; 345 AA.
AC N1ZP05;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Putative D-threonate 4-phosphate dehydrogenase {ECO:0000256|ARBA:ARBA00016951};
DE EC=1.1.1.408 {ECO:0000256|ARBA:ARBA00012116};
GN Name=pdxA2 {ECO:0000313|EMBL:USF30992.1};
GN Synonyms=pdxA {ECO:0000313|EMBL:NDO45367.1};
GN ORFNames=C820_00124 {ECO:0000313|EMBL:EMZ15763.1}, C820_002438
GN {ECO:0000313|EMBL:USF30992.1}, FMM67_00670
GN {ECO:0000313|EMBL:NDO45367.1};
OS Clostridium sp. MD294.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=97138 {ECO:0000313|EMBL:EMZ15763.1};
RN [1] {ECO:0000313|EMBL:EMZ15763.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ASF356 {ECO:0000313|EMBL:EMZ15763.1};
RX PubMed=24723722;
RA Wannemuehler M.J., Overstreet A.M., Ward D.V., Phillips G.J.;
RT "Draft genome sequences of the altered schaedler flora, a defined bacterial
RT community from gnotobiotic mice.";
RL Genome Announc. 2:e00287-e00214(2014).
RN [2] {ECO:0000313|EMBL:NDO45367.1, ECO:0000313|Proteomes:UP000462571}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ASF356 {ECO:0000313|Proteomes:UP000462571}, and MD294
RC {ECO:0000313|EMBL:NDO45367.1};
RA Elie C., Mathieu A., Saliou A., Darnaud M., Leulier F., Tamellini A.;
RT "Draft genome sequences of 15 bacterial species constituting the stable
RT defined intestinal microbiota of the GM15 gnotobiotic mouse model.";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:USF30992.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ASF356 {ECO:0000313|EMBL:USF30992.1};
RA Proctor A., Parvinroo S., Richie T., Jia X., Lee S.T.M., Karp P.D.,
RA Paley S., Kostic A.D., Pierre J.F., Wannemuehler M.J., Phillips G.J.;
RT "Resources to Facilitate Use of the Altered Schaedler Flora (ASF) Mouse
RT Model to Study Microbiome Function.";
RL Submitted (MAY-2022) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the NAD-dependent oxidation and subsequent
CC decarboxylation of D-threonate 4-phosphate to produce dihydroxyacetone
CC phosphate (DHAP). {ECO:0000256|ARBA:ARBA00003324}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-O-phospho-D-threonate + NAD(+) = CO2 + dihydroxyacetone
CC phosphate + NADH; Xref=Rhea:RHEA:52396, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57642, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:136590; EC=1.1.1.408;
CC Evidence={ECO:0000256|ARBA:ARBA00001738};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|ARBA:ARBA00001968};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the PdxA family. PdxA2 subfamily.
CC {ECO:0000256|ARBA:ARBA00009464}.
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DR EMBL; AQFQ01000003; EMZ15763.1; -; Genomic_DNA.
DR EMBL; VIRC01000004; NDO45367.1; -; Genomic_DNA.
DR EMBL; CP097810; USF30992.1; -; Genomic_DNA.
DR AlphaFoldDB; N1ZP05; -.
DR STRING; 97138.C820_00124; -.
DR PATRIC; fig|97138.3.peg.129; -.
DR eggNOG; COG1995; Bacteria.
DR HOGENOM; CLU_040168_0_1_9; -.
DR OrthoDB; 9801783at2; -.
DR Proteomes; UP000012445; Chromosome.
DR Proteomes; UP000462571; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR InterPro; IPR005255; PdxA_fam.
DR NCBIfam; TIGR00557; pdxA; 1.
DR PANTHER; PTHR30004; 4-HYDROXYTHREONINE-4-PHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR30004:SF6; D-THREONATE 4-PHOSPHATE DEHYDROGENASE; 1.
DR Pfam; PF04166; PdxA; 1.
DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:NDO45367.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000012445}.
SQ SEQUENCE 345 AA; 37833 MW; 2E9A57F46BA8653F CRC64;
MSRPIIGITM GDPAGNGAEL SIQALSHKEV YQNCKPIIIG DANCMQQALQ ILGKQNDFKI
NAVKNVSEAL FEFGIIDVYD MELVDIEKRV YGKISEMCGE AAFQYVKKVI ELALSNEIDA
TVTNAISKEA INLAGHHYSG HTEIYADFTK TKKYTMMLAH DELRVVHVST HVSLRDACDK
VKKDRVYEVI KIAYDACKAI GIQNPKIGVA GLNPHCGENG MFGTEEIEQI QPAIDKALSE
GINIPEKKPT PPDTIFSKAL GGWYDIVVAM YHDQGHIPLK VKGFVYNKEL KKWDAVAGIN
VTLGIPVIRV SVDHGTGFDL AGKGVSNEIS LSNSIEYAIL LAKNK
//
