ID L1NBD2_9BACT Unreviewed; 319 AA.
AC L1NBD2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Putative glycerate dehydrogenase {ECO:0000313|EMBL:EKY00799.1};
GN ORFNames=HMPREF9151_01186 {ECO:0000313|EMBL:EKY00799.1};
OS Hoylesella saccharolytica F0055.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Hoylesella.
OX NCBI_TaxID=1127699 {ECO:0000313|EMBL:EKY00799.1, ECO:0000313|Proteomes:UP000010433};
RN [1] {ECO:0000313|EMBL:EKY00799.1, ECO:0000313|Proteomes:UP000010433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0055 {ECO:0000313|EMBL:EKY00799.1,
RC ECO:0000313|Proteomes:UP000010433};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (MAY-2012) 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:EKY00799.1}.
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DR EMBL; AMEP01000082; EKY00799.1; -; Genomic_DNA.
DR RefSeq; WP_009162401.1; NZ_KB290994.1.
DR AlphaFoldDB; L1NBD2; -.
DR STRING; 1127699.HMPREF9151_01186; -.
DR PATRIC; fig|1127699.3.peg.1098; -.
DR HOGENOM; CLU_019796_1_3_10; -.
DR OrthoDB; 9777288at2; -.
DR Proteomes; UP000010433; 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; cd12162; 2-Hacid_dh_4; 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; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 1.
DR PANTHER; PTHR43761:SF1; 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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000010433}.
FT DOMAIN 24..317
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 107..286
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 319 AA; 34740 MW; 7823CF24AB4EEAA7 CRC64;
MKIVVLDGYC ANPGDFSWNE LASFGELTVY DRTSHEEVIA RAHDADILLT NKVILKGDTL
LQLPRLKYIG ILATGYNIIN PEETTRRGIV VSNVPAYSTD SVAQMAFAHI LNITNRVEHY
ADKNRKGEWS RAADFCYWDT PLHELAGKTL GIVGLGNIGC KLTQIARVFG MDVFAVTSKS
SSELPEGIQK TTLDGLLAVS DVLCLTCPLT EDTREMINQQ TLSKMRKGAI LINTSRGPLI
NEADVAAALA EGKLAGYGAD VMSNEPPRPD NPLLAQPNAF ITPHIAWATT EARARLLHTA
IDNVKAFING TPQNVVNPI
//