ID C6DK14_PECCP Unreviewed; 347 AA.
AC C6DK14;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 84.
DE SubName: Full=Alcohol dehydrogenase GroES domain protein {ECO:0000313|EMBL:ACT13397.1};
GN OrderedLocusNames=PC1_2366 {ECO:0000313|EMBL:ACT13397.1};
OS Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=561230 {ECO:0000313|EMBL:ACT13397.1, ECO:0000313|Proteomes:UP000002736};
RN [1] {ECO:0000313|EMBL:ACT13397.1, ECO:0000313|Proteomes:UP000002736}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC1 {ECO:0000313|EMBL:ACT13397.1,
RC ECO:0000313|Proteomes:UP000002736};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Balakrishnan V., Glasner J., Perna N.T.;
RT "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL Submitted (JUL-2009) 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; CP001657; ACT13397.1; -; Genomic_DNA.
DR RefSeq; WP_015840579.1; NC_012917.1.
DR AlphaFoldDB; C6DK14; -.
DR STRING; 561230.PC1_2366; -.
DR KEGG; pct:PC1_2366; -.
DR eggNOG; COG1063; Bacteria.
DR HOGENOM; CLU_026673_11_3_6; -.
DR OMA; VANVGVH; -.
DR OrthoDB; 9773078at2; -.
DR Proteomes; UP000002736; Chromosome.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:UniProt.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08286; FDH_like_ADH2; 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; PTHR42813:SF4; DEHYDROGENASE 1, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR42813; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE; 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|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 8..345
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 347 AA; 37500 MW; A6652CDF54BFFD3C CRC64;
MKAAVYDGNG KISWKEVKDA TLEENTDALV KIIKTTICGS DLHILKGDMP YVPSGRVLGH
EGIGVVEEIG EAVTQFKKGD KVVISAISYC GKCHHCKKGL YCHCESKDGG WVLGNSVNGT
QAEYTRIPHA DNSLIKVPEN VDEESALMLS DILPTGFEVG VLAGEVKPGQ KIAIIGAGPV
GLSVLITSQF YSPAKIIMID MDKSRLEMAK QLGATHTINP QSDDYASICK ELTDGYGVDV
AIECVGIPDT FEMCQEIIAK GGRIANIGVH GKKVDLHMDK LWGSNIQITT GFVCTHSTPM
LMESISSGKI DPKKLISHHF KLDEIEKAYQ VFGNAAKEKA IKIILSK
//