ID A0A0C1S0W1_9ENTR Unreviewed; 380 AA.
AC A0A0C1S0W1;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Erythronate-4-phosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01825};
DE EC=1.1.1.290 {ECO:0000256|HAMAP-Rule:MF_01825};
GN Name=pdxB {ECO:0000256|HAMAP-Rule:MF_01825};
GN ORFNames=P689_119168 {ECO:0000313|EMBL:KIE64197.1};
OS Candidatus Riesia pediculischaeffi PTSU.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Riesia.
OX NCBI_TaxID=1401651 {ECO:0000313|EMBL:KIE64197.1, ECO:0000313|Proteomes:UP000054529};
RN [1] {ECO:0000313|EMBL:KIE64197.1, ECO:0000313|Proteomes:UP000054529}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PTSU {ECO:0000313|EMBL:KIE64197.1,
RC ECO:0000313|Proteomes:UP000054529};
RX PubMed=25213693; DOI=10.1534/g3.114.012567;
RA Boyd B.M., Allen J.M., de Crecy-Lagard V., Reed D.L.;
RT "Genome sequence of Candidatus Riesia pediculischaeffi, endosymbiont of
RT chimpanzee lice, and genomic comparison of recently acquired endosymbionts
RT from human and chimpanzee lice.";
RL G3 (Bethesda) 4:2189-2195(2014).
CC -!- FUNCTION: Catalyzes the oxidation of erythronate-4-phosphate to 3-
CC hydroxy-2-oxo-4-phosphonooxybutanoate. {ECO:0000256|HAMAP-
CC Rule:MF_01825}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-phospho-D-erythronate + NAD(+) = (R)-3-hydroxy-2-oxo-4-
CC phosphooxybutanoate + H(+) + NADH; Xref=Rhea:RHEA:18829,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58538, ChEBI:CHEBI:58766; EC=1.1.1.290;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01825};
CC -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis;
CC pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 2/5.
CC {ECO:0000256|HAMAP-Rule:MF_01825}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01825}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01825}.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. PdxB subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_01825}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01825}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KIE64197.1}.
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DR EMBL; AWXV01000002; KIE64197.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C1S0W1; -.
DR PATRIC; fig|1401651.3.peg.194; -.
DR HOGENOM; CLU_019796_4_0_6; -.
DR OrthoDB; 9770208at2; -.
DR UniPathway; UPA00244; UER00310.
DR Proteomes; UP000054529; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0033711; F:4-phosphoerythronate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd12158; ErythrP_dh; 1.
DR Gene3D; 3.30.1370.170; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR HAMAP; MF_01825; PdxB; 1.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR020921; Erythronate-4-P_DHase.
DR InterPro; IPR024531; Erythronate-4-P_DHase_dimer.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR038251; PdxB_dimer_sf.
DR PANTHER; PTHR43761:SF1; 2-HACID_DH DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR43761; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR Pfam; PF11890; DUF3410; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01825};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01825};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01825};
KW Pyridoxine biosynthesis {ECO:0000256|ARBA:ARBA00023096, ECO:0000256|HAMAP-
KW Rule:MF_01825}.
FT DOMAIN 9..285
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 113..258
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
FT DOMAIN 292..374
FT /note="Erythronate-4-phosphate dehydrogenase dimerisation"
FT /evidence="ECO:0000259|Pfam:PF11890"
FT ACT_SITE 210
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01825"
FT ACT_SITE 239
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01825"
FT ACT_SITE 256
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01825"
FT BINDING 49
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01825"
FT BINDING 70
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01825"
FT BINDING 150
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01825"
FT BINDING 234
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01825"
FT BINDING 259
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01825"
FT BINDING 260
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01825"
SQ SEQUENCE 380 AA; 43834 MW; 52212E25EEA3172E CRC64;
MDGMPNILID KNIPYALELF NKVGRTKIFD NKTLHKKLSK NTDILVVRSV TKVNERLIKN
TGIRFVGSVT SGTDHVDKEW MKNNGVFFCH ADGCNAISVV EYVISALLSQ IDHRNFQLKE
KVFGIVGYGN IGSLLRFYLN SLGITTILYD PIMSPTERKK GEIFVTMEEL VHRSDIISIH
SSLDSSSYHL FNEDILDAIG TNRILINTSR GSLIDNQALA LLFHKGKKIK IILDVWENEP
HISEYLFDRV MLGTPHIAGY SIESKMRGVF QIFEKLNKFL KKEPMSFMKD RFLPIPKFKE
IYLNGSVNQE DLRNLIHLIY NANDDSFLWK KMHERDRKNS FENFRNNYPI RREWSSIEVN
CNDISSFSLL KKIGFIAKSL
//
