ID F4H0M2_CELFA Unreviewed; 338 AA.
AC F4H0M2;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding protein {ECO:0000313|EMBL:AEE44995.1};
GN OrderedLocusNames=Celf_0857 {ECO:0000313|EMBL:AEE44995.1};
OS Cellulomonas fimi (strain ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 /
OS NCIMB 8980 / NCTC 7547).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=590998 {ECO:0000313|EMBL:AEE44995.1, ECO:0000313|Proteomes:UP000008460};
RN [1] {ECO:0000313|EMBL:AEE44995.1, ECO:0000313|Proteomes:UP000008460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 /
RC NCTC 7547 {ECO:0000313|Proteomes:UP000008460};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Mead D., Brumm P.,
RA Woyke T.;
RT "Complete sequence of Cellulomonas fimi ATCC 484.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR EMBL; CP002666; AEE44995.1; -; Genomic_DNA.
DR AlphaFoldDB; F4H0M2; -.
DR STRING; 590998.Celf_0857; -.
DR KEGG; cfi:Celf_0857; -.
DR eggNOG; COG0111; Bacteria.
DR HOGENOM; CLU_019796_1_3_11; -.
DR Proteomes; UP000008460; Chromosome.
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; cd12167; 2-Hacid_dh_8; 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; PTHR10996:SF178; 2-HYDROXYACID DEHYDROGENASE YGL185C-RELATED; 1.
DR PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 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; PS00670; D_2_HYDROXYACID_DH_2; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000008460}.
FT DOMAIN 42..329
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 135..298
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 338 AA; 35932 MW; D2DFE2915F65EAFB CRC64;
MAQPHRPEAL LVMDPGTFAL QFPAPARERL QHLARTGRPL CVSELDSAPA RRRIAEAEVL
LTSWGAPTLT PERVAAAPRL RAVLHCAGSV RGLVSDAVWE RDLLVTSAAD ANARPVAEFT
LAAIIFAGKR APFLAATART RRDDWSFGEL GDLSNRGRTV GIVGFSRIGR RVVELLRVLE
TAAVLVADPV ADPADIAAAG AEHVSLDELL RRSDVVSLHA PALPATHHLL GAAQLALLRD
GATLVNTARG SLVDTAALET ECAAGRLDAV LDVTDPEPLP PTSVLHDLPN VMLTPHVAGS
LGSETQRMSD QALDELERYV HGLPPIAPVT RARLEVLA
//
