ID Q1CXF4_MYXXD Unreviewed; 351 AA.
AC Q1CXF4;
DT 11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 125.
DE SubName: Full=Alcohol dehydrogenase, zinc-containing {ECO:0000313|EMBL:ABF88165.1};
DE EC=1.1.1.1 {ECO:0000313|EMBL:ABF88165.1};
GN Name=adh {ECO:0000313|EMBL:ABF88165.1};
GN OrderedLocusNames=MXAN_6802 {ECO:0000313|EMBL:ABF88165.1};
OS Myxococcus xanthus (strain DK1622).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Myxococcus.
OX NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF88165.1, ECO:0000313|Proteomes:UP000002402};
RN [1] {ECO:0000313|EMBL:ABF88165.1, ECO:0000313|Proteomes:UP000002402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK1622 {ECO:0000313|Proteomes:UP000002402};
RX PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S.,
RA Eisen J.A., Ronning C.M., Barbazuk W.B., Blanchard M., Field C.,
RA Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R.,
RA Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R.,
RA Kaplan H.B.;
RT "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
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; CP000113; ABF88165.1; -; Genomic_DNA.
DR RefSeq; WP_011556727.1; NC_008095.1.
DR AlphaFoldDB; Q1CXF4; -.
DR STRING; 246197.MXAN_6802; -.
DR EnsemblBacteria; ABF88165; ABF88165; MXAN_6802.
DR GeneID; 41363991; -.
DR KEGG; mxa:MXAN_6802; -.
DR eggNOG; COG1063; Bacteria.
DR HOGENOM; CLU_026673_11_3_7; -.
DR OrthoDB; 9774952at2; -.
DR Proteomes; UP000002402; Chromosome.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08285; NADP_ADH; 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; NADP-DEPENDENT ISOPROPANOL DEHYDROGENASE; 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 ECO:0000313|EMBL:ABF88165.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002402};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 7..349
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 351 AA; 37317 MW; 4B07BF6CBF96DD06 CRC64;
MRANVFQAVN RFGIEEVERP RAGAGEAVIR MTMTTVCGTD LHIVRGEYPV RPGLVIGHEP
VGVIEELGPG VTDYRPGQRV LVGAITPCGQ CRACLSSHLS QCGHGAGYEA LGGWRMGNTQ
DGAQAEYIRI PAAQANLAPI PDGLTDEQVI LLSDIASTGF SGAEAGSVRI GDAVVVFAQG
PIGLCASIGA RLMGASLVVG VDGDEARMKM AQRMGVDVVL DHRQQDVVAE VKRLTGGGAD
VAIEALGTQQ TFESALRCLR PAGTLSSLGV YSGKLQLPYD AFSAGLGDYR IVTTLCPGGK
ERMRRLMDLV HHKRVDLSPL ITHRFKLADI QEAYALFGER RDGVFKVAIQ P
//
