ID A0A1G0XR48_9BACT Unreviewed; 376 AA.
AC A0A1G0XR48;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Erythronate-4-phosphate dehydrogenase {ECO:0000313|EMBL:OGV36131.1};
GN ORFNames=A2X48_01200 {ECO:0000313|EMBL:OGV36131.1};
OS Lentisphaerae bacterium GWF2_49_21.
OC Bacteria; Lentisphaerota.
OX NCBI_TaxID=1798573 {ECO:0000313|EMBL:OGV36131.1, ECO:0000313|Proteomes:UP000178513};
RN [1] {ECO:0000313|EMBL:OGV36131.1, ECO:0000313|Proteomes:UP000178513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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:OGV36131.1}.
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DR EMBL; MHBH01000083; OGV36131.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0XR48; -.
DR STRING; 1798573.A2X48_01200; -.
DR Proteomes; UP000178513; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0033711; F:4-phosphoerythronate dehydrogenase activity; IEA:InterPro.
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-KW.
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; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 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};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Pyridoxine biosynthesis {ECO:0000256|ARBA:ARBA00023096}.
FT DOMAIN 31..284
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 111..257
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
FT DOMAIN 304..359
FT /note="Erythronate-4-phosphate dehydrogenase dimerisation"
FT /evidence="ECO:0000259|Pfam:PF11890"
SQ SEQUENCE 376 AA; 41804 MW; BDA64FC0201E92D5 CRC64;
MKIVCDNKIP FLKGVLEPYA EVVYLPGAKI AKADLADADG LIVRTRTKCN KELLSGTKVK
FVATATIGFD HIDANYCESN RIFWTNAAGC NSASVAQYVA SAILNLAVEN KFSLSEKTLG
IIGVGNVGSK VAKFAKTAGM KVLLNDPPRA RKEGDETSFV SLERILAESD IITLHVPLNM
TGPDKTYHLA DKIFFNSIAK CAWLINSSRG EVCDTMELKN ILKTSRIAGA ILDVWENEPE
IDLDLLGLAK FATPHIAGYS TDGKANGTSM SVQSLAKFFE IKQLENWYPR EVPKPENITI
KTGCKGKAKE QILLEAVKFT YDVREDDRRL RASPRTFEKL REEYPLRREF KIFKITSHDL
PGDCLKIFNE LGFQIE
//
