ID A6SYB5_JANMA Unreviewed; 334 AA.
AC A6SYB5;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Zinc-type alcohol dehydrogenase-like protein {ECO:0000256|RuleBase:RU364000};
GN OrderedLocusNames=mma_1572 {ECO:0000313|EMBL:ABR88529.1};
OS Janthinobacterium sp. (strain Marseille) (Minibacterium massiliensis).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=375286 {ECO:0000313|EMBL:ABR88529.1, ECO:0000313|Proteomes:UP000006388};
RN [1] {ECO:0000313|EMBL:ABR88529.1, ECO:0000313|Proteomes:UP000006388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Marseille {ECO:0000313|EMBL:ABR88529.1,
RC ECO:0000313|Proteomes:UP000006388};
RX PubMed=17722982; DOI=10.1371/journal.pgen.0030138;
RA Audic S., Robert C., Campagna B., Parinello H., Claverie J.-M., Raoult D.,
RA Drancourt M.;
RT "Genome analysis of Minibacterium massiliensis highlights the convergent
RT evolution of water-living bacteria.";
RL PLoS Genet. 3:1454-1463(2007).
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Quinone oxidoreductase subfamily.
CC {ECO:0000256|RuleBase:RU364000}.
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; CP000269; ABR88529.1; -; Genomic_DNA.
DR RefSeq; WP_012079427.1; NC_009659.1.
DR AlphaFoldDB; A6SYB5; -.
DR STRING; 375286.mma_1572; -.
DR KEGG; mms:mma_1572; -.
DR eggNOG; COG0604; Bacteria.
DR HOGENOM; CLU_026673_3_0_4; -.
DR OrthoDB; 9785812at2; -.
DR Proteomes; UP000006388; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08252; AL_MDR; 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; IPR013154; ADH-like_N.
DR InterPro; IPR014182; ADH_Zn_typ-1.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR NCBIfam; TIGR02817; adh_fam_1; 1.
DR PANTHER; PTHR44154; QUINONE OXIDOREDUCTASE; 1.
DR PANTHER; PTHR44154:SF1; QUINONE OXIDOREDUCTASE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU364000};
KW Oxidoreductase {ECO:0000256|RuleBase:RU364000};
KW Reference proteome {ECO:0000313|Proteomes:UP000006388};
KW Zinc {ECO:0000256|RuleBase:RU364000}.
FT DOMAIN 16..331
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 334 AA; 36250 MW; A3C895DF2AF90119 CRC64;
MKAIAYKKAL PISDAQALLD VTLPDPVASG HDLLVEVKAI SVNPVDVKVR SSANPPDGEY
KVIGWDAAGI VRAVGDAVTL FKPGDRVFYA GSIARPGTNS ELHLVDEFIS GHMPESLDFA
QAAALPLTAI TAWELLFERL EIGRDNKEAI LIIGAAGGVG SILVQLARQL TGLTVIATAS
RPQTQQWVRE LGAHHVIDHA QPLSQELKKI GIENVKYVAS LNQTDQHFSE IVESLAPQGK
LALIDDPAAL DIRLLKRKSI SLHWEFMFTR ALFGTPDMHK QHELLNEVAR LIDAGIVKTT
VAEHFGTINA ANLRRAHELL ESNSSKGKIV LEGF
//
