ID G9YJ23_9FIRM Unreviewed; 315 AA.
AC G9YJ23;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Putative glycerate dehydrogenase {ECO:0000313|EMBL:EHM39067.1};
GN ORFNames=HMPREF0080_01667 {ECO:0000313|EMBL:EHM39067.1};
OS Anaeroglobus geminatus F0357.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Anaeroglobus.
OX NCBI_TaxID=861450 {ECO:0000313|EMBL:EHM39067.1, ECO:0000313|Proteomes:UP000005481};
RN [1] {ECO:0000313|EMBL:EHM39067.1, ECO:0000313|Proteomes:UP000005481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0357 {ECO:0000313|EMBL:EHM39067.1,
RC ECO:0000313|Proteomes:UP000005481};
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., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
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:EHM39067.1}.
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DR EMBL; AGCJ01000073; EHM39067.1; -; Genomic_DNA.
DR RefSeq; WP_006790634.1; NZ_JH417605.1.
DR AlphaFoldDB; G9YJ23; -.
DR STRING; 861450.HMPREF0080_01667; -.
DR GeneID; 85019819; -.
DR PATRIC; fig|861450.3.peg.1540; -.
DR eggNOG; COG0111; Bacteria.
DR HOGENOM; CLU_019796_1_3_9; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000005481; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR CDD; cd12161; GDH_like_1; 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; 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 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000005481}.
FT DOMAIN 12..310
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 111..284
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 315 AA; 33976 MW; F8A67F36F0728A40 CRC64;
MKIVLLESLG ISDEILQSYA EALEKEGHRF TAYERTEDTA RQIEEAKDSD IIIIANMPLK
GEVIKACPDL KYIDVAFTGV DHVDLEAAKG KGIKVSNASG YSTVAVAELT IAMMLNLLRN
VRAVEDACRN GGTKSGLVGS ELEGKTVALF GTGAIGSRVA ELAHAFGAKI IAYNGFSKKD
DTDLITYLPI KELMEQADIV SLHCPVTDQS RNIINAKTLA YMKPTAYLIN EARGPVVDSR
ALADALNSGK IAGAGIDVFE TEPPLNTAHP LLHAKNTIVT PHVAFATRES MRKRAAIVFD
NIHTFLAGNQ QNIIL
//
