ID A0A1E3L1F9_9BACL Unreviewed; 350 AA.
AC A0A1E3L1F9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=(R,R)-butanediol dehydrogenase {ECO:0000313|EMBL:ODP27622.1};
DE EC=1.1.1.- {ECO:0000313|EMBL:ODP27622.1};
DE EC=1.1.1.303 {ECO:0000313|EMBL:ODP27622.1};
DE EC=1.1.1.4 {ECO:0000313|EMBL:ODP27622.1};
GN Name=butB {ECO:0000313|EMBL:ODP27622.1};
GN ORFNames=PTI45_02992 {ECO:0000313|EMBL:ODP27622.1};
OS Paenibacillus nuruki.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1886670 {ECO:0000313|EMBL:ODP27622.1, ECO:0000313|Proteomes:UP000094578};
RN [1] {ECO:0000313|EMBL:ODP27622.1, ECO:0000313|Proteomes:UP000094578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TI45-13ar {ECO:0000313|EMBL:ODP27622.1,
RC ECO:0000313|Proteomes:UP000094578};
RA Kim S.-J.;
RT "Genome sequencing of Paenibacillus sp. TI45-13ar, isolated from Korean
RT traditional nuruk.";
RL Submitted (AUG-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}.
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:ODP27622.1}.
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DR EMBL; MDER01000049; ODP27622.1; -; Genomic_DNA.
DR RefSeq; WP_069328396.1; NZ_OY725677.1.
DR AlphaFoldDB; A0A1E3L1F9; -.
DR STRING; 1886670.PTI45_02992; -.
DR PATRIC; fig|1886670.3.peg.3042; -.
DR Proteomes; UP000094578; Unassembled WGS sequence.
DR GO; GO:0000721; F:(R,R)-butanediol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0052587; F:diacetyl reductase ((R)-acetoin forming) activity; IEA:UniProtKB-EC.
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; 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.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ODP27622.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000094578};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 8..346
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 350 AA; 37519 MW; 6678F4EBF9CED1D4 CRC64;
MQALRWHGVK DLRVETIEEP QASAGKVKIK IEWCGICGSD LHEYAAGPIF ISQGTNHPLT
HEQAPVVMGH EFSGQVVEVG EGVTKVKAGD RVVVEPIFAC GKCTACKQGK YNLCEHMGFL
GLAGGGGGFS EYVAADEHMV HKIPDSVSYE QGALVEPSAV ALYAVRQSQL KVGDRAVVFG
AGPIGLLVIE ALKASGAAEI YAVELSEERR QTAESLGAIG LNPAEVDVVA EIHRLTNGGA
DVAYEVTGVP VVLTQAIQST KLSGQIMIVS IFEKEAPIHP NQIVMQERNI TGIIGYRDVF
PAVISLMSQG YFSSEKLVTK RIALNEIVEQ GFEALLKEKN QVKIMVSPSL
//
