ID D3AR29_9CLOT Unreviewed; 339 AA.
AC D3AR29;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=4-phosphoerythronate dehydrogenase {ECO:0000313|EMBL:EFC95729.1};
DE EC=1.1.1.290 {ECO:0000313|EMBL:EFC95729.1};
GN Name=pdxB {ECO:0000313|EMBL:EFC95729.1};
GN ORFNames=CLOSTHATH_06085 {ECO:0000313|EMBL:EFC95729.1};
OS Hungatella hathewayi DSM 13479.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Hungatella.
OX NCBI_TaxID=566550 {ECO:0000313|EMBL:EFC95729.1, ECO:0000313|Proteomes:UP000004968};
RN [1] {ECO:0000313|EMBL:EFC95729.1, ECO:0000313|Proteomes:UP000004968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13479 {ECO:0000313|EMBL:EFC95729.1,
RC ECO:0000313|Proteomes:UP000004968};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC 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:EFC95729.1}.
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DR EMBL; ACIO01000687; EFC95729.1; -; Genomic_DNA.
DR RefSeq; WP_006776499.1; NZ_GG667802.1.
DR AlphaFoldDB; D3AR29; -.
DR HOGENOM; CLU_019796_1_3_9; -.
DR Proteomes; UP000004968; Unassembled WGS sequence.
DR GO; GO:0033711; F:4-phosphoerythronate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR CDD; cd12167; 2-Hacid_dh_8; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR42789; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR PANTHER; PTHR42789:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 31..322
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 124..296
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 339 AA; 37286 MW; 547D4C0882AF2528 CRC64;
MRDKLKPIKI LVSIPAGEMR DSFFSEALSA RLEQLGCVEW NTNTEQFSEE ELAEKLSGVD
ICISGWGNTP FYEKTLKYAD KLKLIAHIGG SVRPMVGDAA FERGIRVCSG NRVFAESVAE
GVLTYMLCSL RKIGEYEARM AAGEWPSLIG TRGLLGRSVG LVGYGMIAEY LVKFLKPFGC
RILVSSRHIS EEELAAAGIE AASAEEIFRT CDIVSLHNSL TMRTKHSIGA ELLNSMKDGA
LLVNTARGAL IDEEALVSVL KERSVWAALD VYETEPLPMD SPLRDCERVL LMPHAAGPTA
DRRYAVTSYV LDDMERFLNG ENLDCEIDFA RAGTMTTVV
//
