ID B5GZE3_STRCL Unreviewed; 729 AA.
AC B5GZE3;
DT 14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2008, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Bi-domain oxidoreductase {ECO:0000313|EMBL:EFG10717.1};
GN ORFNames=SCLAV_5650 {ECO:0000313|EMBL:EFG10717.1};
OS Streptomyces clavuligerus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1901 {ECO:0000313|EMBL:EFG10717.1, ECO:0000313|Proteomes:UP000002357};
RN [1] {ECO:0000313|EMBL:EFG10717.1, ECO:0000313|Proteomes:UP000002357}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 /
RC NRRL 3585 / VKM Ac-602 {ECO:0000313|Proteomes:UP000002357};
RX PubMed=20624727; DOI=10.1093/gbe/evq013;
RA Medema M.H., Trefzer A., Kovalchuk A., van den Berg M., Mueller U.,
RA Heijne W., Wu L., Alam M.T., Ronning C.M., Nierman W.C., Bovenberg R.A.L.,
RA Breitling R., Takano E.;
RT "The sequence of a 1.8-mb bacterial linear plasmid reveals a rich
RT evolutionary reservoir of secondary metabolic pathways.";
RL Genome Biol. Evol. 2:212-224(2010).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM000913; EFG10717.1; -; Genomic_DNA.
DR RefSeq; WP_003957311.1; NZ_WMCA01000111.1.
DR STRING; 1901.BB341_00320; -.
DR GeneID; 61468203; -.
DR KEGG; sclf:BB341_00320; -.
DR eggNOG; COG0673; Bacteria.
DR eggNOG; COG1063; Bacteria.
DR OrthoDB; 9792935at2; -.
DR Proteomes; UP000002357; Chromosome.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR CDD; cd08255; 2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_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; 2.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43350:SF22; D-GULOSIDE 3-DEHYDROGENASE; 1.
DR PANTHER; PTHR43350; NAD-DEPENDENT ALCOHOL DEHYDROGENASE; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR Pfam; PF01408; GFO_IDH_MocA; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000002357}.
FT DOMAIN 182..300
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
FT DOMAIN 408..528
FT /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01408"
SQ SEQUENCE 729 AA; 76903 MW; BD1D65DE7CBBAE3D CRC64;
MKQVVQNYKS GELALLDVPE PGCAPGGVLV RSAYSLISTG TELMKVSEAG MSMLGKARSR
PDQVAKVMQS VAVNGVPATY RKVMGKLDSY TPLGYSLCGV VEEVGAGVDE VKAGDLVACA
GNEHALHAEL NWVPKNLFAR VPDGLAPRHA AFGTVGSIAL QGVRRGEPQL GEVALVIGLG
LIGQLVAQLL TASGVRVVGV DPDPARCALA ARLGAAACGD PASTAVAAAV AELTDGHGVD
QVYLAAGGGS NQPVELAARL SRDRGRVVDI GKCRLDLPWN AYYEKELDVR FSRSYGPGRY
DPEYELEGRD YPIGYVRWTE RRNLACFLDL TARGGVDVEP LISHIAGFDD AVETYRRLKD
GELEAVAVLF RYPGHTEEPK AAPAVAVPAV RRSGAAPAAT GTGGAPVRLA FVGAGNYATS
MLLPHLARRD GVELSAVVTT TALSGANARR KFGFARATTD LDTVLGDPAV DAVFVVTRHS
SHADLTRRAL LAGKAVFVEK PLALDQDELA GVLAAVEESG NDRLQVGFNR RFAPLLNEAR
TRFGTRSGPA SLRYLVNAGR LDHGSWYLRQ DTEGSRFAGE GGHFIDTASW LLGADPVSVY
AVATPGTEDL QIVLGYPDGS TATVSYVTTG APGFPKETLD LVADGKVLRL DDFVRAAVYD
DRRKRWAGPR LPQARDKGQS AQLAAFIRAL RTGGPMPVPL ESLAATTAAT LAVRDGLVSG
APVTLARAR
//
