ID F9MQW8_9FIRM Unreviewed; 315 AA.
AC F9MQW8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Putative glyoxylate reductase {ECO:0000313|EMBL:EGS32124.1};
GN ORFNames=HMPREF1040_0501 {ECO:0000313|EMBL:EGS32124.1};
OS Megasphaera sp. UPII 135-E.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Megasphaera.
OX NCBI_TaxID=1000569 {ECO:0000313|EMBL:EGS32124.1, ECO:0000313|Proteomes:UP000004137};
RN [1] {ECO:0000313|EMBL:EGS32124.1, ECO:0000313|Proteomes:UP000004137}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UPII 135-E {ECO:0000313|EMBL:EGS32124.1,
RC ECO:0000313|Proteomes:UP000004137};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (JUN-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:EGS32124.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AFUG01000043; EGS32124.1; -; Genomic_DNA.
DR RefSeq; WP_007393148.1; NZ_AFUG01000043.1.
DR AlphaFoldDB; F9MQW8; -.
DR eggNOG; COG0111; Bacteria.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000004137; 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:UP000004137}.
FT DOMAIN 26..311
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; 33737 MW; A8B8AA129A4C460F CRC64;
MKVVLLESLG ISSDLLATYA DKLKAQGHSF AAYERTDDVS VQIEEANDAD ILIIANMPLK
GEVIRACPHL KYIDVAFTGV DHVDLAAAQE RGIRVSNASG YSTVAVAELT IAMMLHLLRY
VAQVDAACRA GGTKAGFIGY ELEGKTVGLF GTGAIGHRVA ELVHAFGAKV IAYNGFSHKE
STALITYVSL EEVMSMADII SLHCPVTEQS RGLINAKTLS YMKPSAILIN EARGPVVDSQ
ALADALNTGK IAGAGIDVFE VEPPIDTKHP LLHSKNTIVT PHVAFATHES MKKRAVIVFE
NIDNFLAGKQ LNIIL
//
