ID A0A1Y4CF90_9FIRM Unreviewed; 315 AA.
AC A0A1Y4CF90;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Hydroxyacid dehydrogenase {ECO:0000313|EMBL:OUO45366.1};
GN ORFNames=B5F80_08730 {ECO:0000313|EMBL:OUO45366.1};
OS Megasphaera sp. An286.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Megasphaera.
OX NCBI_TaxID=1965622 {ECO:0000313|EMBL:OUO45366.1, ECO:0000313|Proteomes:UP000195529};
RN [1] {ECO:0000313|EMBL:OUO45366.1, ECO:0000313|Proteomes:UP000195529}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An286 {ECO:0000313|EMBL:OUO45366.1,
RC ECO:0000313|Proteomes:UP000195529};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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:OUO45366.1}.
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DR EMBL; NFIY01000018; OUO45366.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4CF90; -.
DR Proteomes; UP000195529; 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:UP000195529}.
FT DOMAIN 16..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; 33808 MW; 562DF9A1D3894E7B CRC64;
MKIVLLESLG ISQELLDSYV KPLREQGHEF AAYERNDDPA VQIEEAKDAD ILIIANMPLK
GEVINACPNL KYINVAFTGV DHVDLEAAKA KGVKVSNASG YSTVAVAELT IAMILDLLRY
VPQVDAACRA GGTKAGFIGA ELEGKTVGLI GTGAIGHRVA ELVHAFGAKV IAYNGFSHKA
DTELIKYVPL KELMEQSDIV SLHCPVTDQS RGMINAETLS YMKPTAFLVN EARGPVVDSQ
ALADALNSGK IAGAGIDVFE NEPPLDTNHP LLHSKNTIVT PHVAFATKES MEKRAVIVFD
NIDAYMAGNQ KNVIL
//
