ID A0A0T6ARS2_9BACT Unreviewed; 319 AA.
AC A0A0T6ARS2;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding protein {ECO:0000313|EMBL:KRT77661.1};
GN ORFNames=XU14_C0007G0002 {ECO:0000313|EMBL:KRT77661.1};
OS Armatimonadetes bacterium CSP1-3.
OC Bacteria; Armatimonadota.
OX NCBI_TaxID=1640515 {ECO:0000313|EMBL:KRT77661.1, ECO:0000313|Proteomes:UP000051026};
RN [1] {ECO:0000313|EMBL:KRT77661.1, ECO:0000313|Proteomes:UP000051026}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSP1-3 {ECO:0000313|EMBL:KRT77661.1};
RA Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT "Critical biogeochemical functions in the subsurface are associated with
RT bacteria from new phyla and little studied lineages.";
RL Submitted (MAY-2015) 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:KRT77661.1}.
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DR EMBL; LDXQ01000007; KRT77661.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T6ARS2; -.
DR PATRIC; fig|1640515.3.peg.417; -.
DR Proteomes; UP000051026; 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; cd05300; 2-Hacid_dh_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; 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; 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.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 9..313
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 107..282
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 319 AA; 35241 MW; DFF00EB362BC87CE CRC64;
MNADPLRILV VADVAERHLS MIREAAPQAQ IEQTVDRGRV VRQAENADVI VGWNVPREAV
QQAKHLRWIH STAAGVDQLL HPEVVQRDII VTDSSGIHAE PITEHVLAVM LAFARRLPVA
TRNQMTHRWD RASVIGEELW GKTVGILGLG SIGREVAARC QAFGMRVIGT KRTPAAVPHV
DQVLPPDGLD EVLRAADYLV IILPLTEQTR GLIGARELGL MKPTAYLINV ARGAIVQEAD
LIAALRPGRL RGAGLDVFER EPLPQDSPLW EMEQVILTPH VSGAVPDYYD RALPLFCENL
RRFLTGAPLL NMVDKRQGY
//
