ID A0A1I4Q3R6_9BACI Unreviewed; 349 AA.
AC A0A1I4Q3R6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=(R,R)-butanediol dehydrogenase / meso-butanediol dehydrogenase / diacetyl reductase {ECO:0000313|EMBL:SFM34677.1};
GN ORFNames=SAMN04488054_13620 {ECO:0000313|EMBL:SFM34677.1};
OS Salibacterium qingdaonense.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae.
OX NCBI_TaxID=266892 {ECO:0000313|EMBL:SFM34677.1, ECO:0000313|Proteomes:UP000199668};
RN [1] {ECO:0000313|EMBL:SFM34677.1, ECO:0000313|Proteomes:UP000199668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6134 {ECO:0000313|EMBL:SFM34677.1,
RC ECO:0000313|Proteomes:UP000199668};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU361277};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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DR EMBL; FOTY01000036; SFM34677.1; -; Genomic_DNA.
DR RefSeq; WP_076572473.1; NZ_FOTY01000036.1.
DR AlphaFoldDB; A0A1I4Q3R6; -.
DR STRING; 266892.SAMN04488054_13620; -.
DR OrthoDB; 9770238at2; -.
DR Proteomes; UP000199668; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08233; butanediol_DH_like; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR006189; CHASE_dom.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR43161:SF23; (R,R)-BUTANEDIOL DEHYDROGENASE-RELATED; 1.
DR PANTHER; PTHR43161; SORBITOL DEHYDROGENASE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
DR PROSITE; PS50839; CHASE; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000199668};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 235..349
FT /note="CHASE"
FT /evidence="ECO:0000259|PROSITE:PS50839"
SQ SEQUENCE 349 AA; 37493 MW; 300A63DDA10C7BA1 CRC64;
MKAAVWYGKK DLRVEEIELK QTKDTDVKVR VAWAGICGSD LHEYEEGPVF VPNEKEDPLT
GEIAPLTMGH EFAGVIEEVG PKVTKYKVGD RVVINPTITY GNKSEDLDPY DGFSFIGLHG
DGGFTKYANV PEDNVYLLPE SLTLQDGALV EPTAVAVQAV KEGKLQFGDT VAVFGAGPIG
LVTIIAAKAA GASKIIALDL SETRIEKAKE LGATHVVNSS EQDAVTAIKE IVPDGVDVSF
EVAGVAPTFK QAIDATRARG TMVIVSIFAR EIEWNPIQLT NTGVKVTSTI AYTPTTFQQT
VDLMGTGQLK PQGIITDQIQ LDDIVENGFE ALTNDKSQAK ILVELSGEK
//