ID A0A257W5I0_9BACT Unreviewed; 324 AA.
AC A0A257W5I0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Dehydrogenase {ECO:0000313|EMBL:OYW17434.1};
GN ORFNames=B7Z55_12530 {ECO:0000313|EMBL:OYW17434.1};
OS Planctomycetales bacterium 12-60-4.
OC Bacteria; Planctomycetota; Planctomycetia; Planctomycetales.
OX NCBI_TaxID=1970541 {ECO:0000313|EMBL:OYW17434.1, ECO:0000313|Proteomes:UP000216774};
RN [1] {ECO:0000313|EMBL:OYW17434.1, ECO:0000313|Proteomes:UP000216774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12-60-4 {ECO:0000313|EMBL:OYW17434.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:OYW17434.1}.
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DR EMBL; NCBX01000886; OYW17434.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A257W5I0; -.
DR Proteomes; UP000216774; 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 GO; GO:0003714; F:transcription corepressor activity; IEA:InterPro.
DR CDD; cd05299; CtBP_dh; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR043322; CtBP.
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}.
FT DOMAIN 20..316
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 110..284
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 324 AA; 34639 MW; 0540B60339674408 CRC64;
MSQFRVLITD RAWPDTELER RILDAIGATI VEPAGTDEAS LCAAAADVDA IATNWAKVTT
SVINAAPRCR IVARLGIGVD NIDIPAASAR GIPVTNCPDY CVAEVADHAL GMLLALARHI
AFFHGRTKRG EYSLQAGQAG LRRLSTQTLG LFGLGRIGRE LASRARALGL NIIAHTSSGD
DYGVGCRMVS FDMLLAESDY LSLHAPLTAA THHKFNAAAF ANMRATAMLI NTSRGGLIDH
AALWTALQQG QVAGAALDVF EPEPPDLTEP LFQDERVIVT PHAAFVSAES LADLRNRVMG
QVAAALTDRR PENVLNPHIY DKTA
//
