ID A0A0N8K677_9RHOB Unreviewed; 310 AA.
AC A0A0N8K677;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Gyoxylate/hydroxypyruvate reductase A {ECO:0000313|EMBL:KPP88169.1};
DE EC=1.1.1.79 {ECO:0000313|EMBL:KPP88169.1};
DE EC=1.1.1.81 {ECO:0000313|EMBL:KPP88169.1};
GN Name=ghrA {ECO:0000313|EMBL:KPP88169.1};
GN ORFNames=HLUCCO07_13630 {ECO:0000313|EMBL:KPP88169.1};
OS Rhodobacteraceae bacterium HLUCCO07.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1666914 {ECO:0000313|EMBL:KPP88169.1, ECO:0000313|Proteomes:UP000050369};
RN [1] {ECO:0000313|EMBL:KPP88169.1, ECO:0000313|Proteomes:UP000050369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLUCCO07 {ECO:0000313|EMBL:KPP88169.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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:KPP88169.1}.
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DR EMBL; LJSU01000007; KPP88169.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N8K677; -.
DR STRING; 1666914.HLUCCO07_13630; -.
DR PATRIC; fig|1666914.4.peg.358; -.
DR Proteomes; UP000050369; Unassembled WGS sequence.
DR GO; GO:0030267; F:glyoxylate reductase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0016618; F:hydroxypyruvate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR CDD; cd12164; GDH_like_2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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; PTHR43333; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43333:SF1; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 4: Predicted;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:KPP88169.1}; Pyruvate {ECO:0000313|EMBL:KPP88169.1}.
FT DOMAIN 123..275
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 310 AA; 33534 MW; 435CBEE9701AC152 CRC64;
MTANILFAAR PDRWAEYEKP LRDALDKTGV SYSLSTEFPP EEVDYIIYAP NSEVQDFTPF
TRAKAVLNLW AGVEHVAPNP TLDIPLARMV GGGLTEGMVE WVTGHTLRHH LGMDAHIVNP
SHHWKPSPPP LAYERAVTVL GLGELGRACA TTLAGLGFRV SGWSRSPKSI ENVTCHHGES
GLRVALQDAE IIILLLPNTP ATENTLNAET LALTAPGAFV INPGRGTLID DDALLAALDS
GRVAHATLDV FRQEPLPADH PYWSHPKVTV TPHIASDTRP GPASEVIAEN VRRGETGAPF
LHLVDRSAGY
//
