ID A0PSA5_MYCUA Unreviewed; 341 AA.
AC A0PSA5;
DT 09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 102.
DE SubName: Full=Dehydrogenase {ECO:0000313|EMBL:ABL05224.1};
GN OrderedLocusNames=MUL_2962 {ECO:0000313|EMBL:ABL05224.1};
OS Mycobacterium ulcerans (strain Agy99).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium ulcerans group.
OX NCBI_TaxID=362242 {ECO:0000313|EMBL:ABL05224.1, ECO:0000313|Proteomes:UP000000765};
RN [1] {ECO:0000313|EMBL:ABL05224.1, ECO:0000313|Proteomes:UP000000765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Agy99 {ECO:0000313|EMBL:ABL05224.1,
RC ECO:0000313|Proteomes:UP000000765};
RX PubMed=17210928; DOI=10.1101/gr.5942807;
RA Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA Johnson P.D., Davies J.K., Jenkin G.A., Small P.L., Jones L.M., Tekaia F.,
RA Laval F., Daffe M., Parkhill J., Cole S.T.;
RT "Reductive evolution and niche adaptation inferred from the genome of
RT Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL Genome Res. 17:192-200(2007).
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; CP000325; ABL05224.1; -; Genomic_DNA.
DR AlphaFoldDB; A0PSA5; -.
DR KEGG; mul:MUL_2962; -.
DR eggNOG; COG1063; Bacteria.
DR HOGENOM; CLU_026673_11_2_11; -.
DR OMA; YTAQCDT; -.
DR Proteomes; UP000000765; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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: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 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..339
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 341 AA; 34465 MW; BB5B06BC2B8302DD CRC64;
MRTVVIDGPG SIRVDNRPDP ALPGSDGVIV VVSAAGICGS DLHFYEGEYP LAEPVALGHE
AVGTVVEKGP DVHTVEVGDQ VMVSSVAGCG ACAGCATRDP AMCVSGPQIF GSGALGGAQA
DLLAVPATDF QVLKIPAAIT TEQALLLTDN LATGWAAARR ADIPFGATVA VIGLGAVGLC
AVRSALAQGA ATVFAVDRVQ GRLQRAAEWG ATAVASPAAE AIVAATSGRG ADSVIDAVDT
DASMTDALNA VRAGGTVSVV GVHDLQPFPL PALTCLLRSI TLRLTIAPVQ RTWSELIPLL
ESGRLDVDGI FTTSLPLDEA AKGYSIAGSR SGNDVKVLLK V
//