ID U5VW37_9ACTN Unreviewed; 391 AA.
AC U5VW37;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:AGZ41022.1};
GN ORFNames=AFR_13680 {ECO:0000313|EMBL:AGZ41022.1};
OS Actinoplanes friuliensis DSM 7358.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=1246995 {ECO:0000313|EMBL:AGZ41022.1, ECO:0000313|Proteomes:UP000017746};
RN [1] {ECO:0000313|EMBL:AGZ41022.1, ECO:0000313|Proteomes:UP000017746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7358 {ECO:0000313|EMBL:AGZ41022.1,
RC ECO:0000313|Proteomes:UP000017746};
RX PubMed=24637369; DOI=10.1016/j.jbiotec.2014.03.011;
RA Ruckert C., Szczepanowski R., Albersmeier A., Goesmann A., Fischer N.,
RA Steinkamper A., Puhler A., Biener R., Schwartz D., Kalinowski J.;
RT "Complete genome sequence of the actinobacterium Actinoplanes friuliensis
RT HAG 010964, producer of the lipopeptide antibiotic friulimycin.";
RL J. Biotechnol. 178:41-42(2014).
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|RuleBase:RU361277}.
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DR EMBL; CP006272; AGZ41022.1; -; Genomic_DNA.
DR RefSeq; WP_023361081.1; NC_022657.1.
DR AlphaFoldDB; U5VW37; -.
DR STRING; 1246995.AFR_13680; -.
DR KEGG; afs:AFR_13680; -.
DR PATRIC; fig|1246995.3.peg.2778; -.
DR eggNOG; COG1063; Bacteria.
DR HOGENOM; CLU_026673_11_3_11; -.
DR OrthoDB; 3399630at2; -.
DR Proteomes; UP000017746; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08283; FDH_like_1; 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 PANTHER; PTHR42813:SF2; DEHYDROGENASE, ZINC-CONTAINING, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G02810)-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 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 Reference proteome {ECO:0000313|Proteomes:UP000017746};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 26..150
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 198..267
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 391 AA; 42178 MW; E944DA1BF7B07FC6 CRC64;
MRANTWSGRN KVEVRDVPDP KILNNRDAIV RITSTAICGS DLHLVDGYVP TMQDGDILGH
EFMGEVIEVG SGVPGEKLRV GDRVVVPFPI ACGACAACAA ELYSCCENTN PNAGIAEKMF
GHPVAGIFGY SHLTGGFAGG QAQYARVPFA DVGPLKIESD LTDEQVLFLS DILPTGYMGA
EMCDIQSSDV VAVWGAGPVG QFAMDSARVL GAAKVIAIDK EPYRLQMAER AGHIPVNFDE
VDVRSTLLEL TGGRGPDKCI DAVGLEADHG SAHIAAYDRV KQAVRSETER PHALRQAIMS
CRSGGVVSVI GVYGGLLDKF PAGAWMNRSL TLRTGQCHVQ RYMKPLLERI ERGEIDPTRI
ITHTLALDEA EQGFNLFKNK QDNCEKVVLK P
//
