ID Q1CYS5_MYXXD Unreviewed; 406 AA.
AC Q1CYS5;
DT 11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 130.
DE SubName: Full=Oxidoreductase, zinc-binding dehydrogenase family {ECO:0000313|EMBL:ABF86936.1};
GN OrderedLocusNames=MXAN_6323 {ECO:0000313|EMBL:ABF86936.1};
OS Myxococcus xanthus (strain DK1622).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Myxococcus.
OX NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF86936.1, ECO:0000313|Proteomes:UP000002402};
RN [1] {ECO:0000313|EMBL:ABF86936.1, 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|RuleBase:RU361277}.
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DR EMBL; CP000113; ABF86936.1; -; Genomic_DNA.
DR RefSeq; WP_011556256.1; NC_008095.1.
DR AlphaFoldDB; Q1CYS5; -.
DR STRING; 246197.MXAN_6323; -.
DR EnsemblBacteria; ABF86936; ABF86936; MXAN_6323.
DR GeneID; 41363539; -.
DR KEGG; mxa:MXAN_6323; -.
DR eggNOG; COG1063; Bacteria.
DR HOGENOM; CLU_026673_11_3_7; -.
DR OrthoDB; 9774952at2; -.
DR Proteomes; UP000002402; 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 InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR42813:SF7; ALCOHOL DEHYDROGENASE (ZN-DEPENDENT)-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 Reference proteome {ECO:0000313|Proteomes:UP000002402};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 8..393
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 406 AA; 43378 MW; 5856B044592C288C CRC64;
MKAVVFHGIG DIRLDDVEEP RIEKSTDAIV RLTASAICGT DLHMIRGTMP GMKPGTILGH
EGVGVIEALG DDVRNLNIGD RVVIPSTIAC GNCSYCRAGY HAQCNDANPN GPSAGTAFFG
GPQETGPFHG MQAEKVRVPF ANVGLVRIPE GVSDEQAILI SDIFPTGYMG AELAEIKPGD
TVAVFGCGPV GLFAIVSAKL LGAGRVFAID CHEDRLDLAR AQGAEVINFE EEDPLETLKR
LTNGIGVDRA IDAVGVDAMH PHHGPAAKKA HQEKAEFKRE VKEAAPKTNP KGDNWVPGDA
PAQALMWAVE GLAKAGTLSI IGVYPAQVRT FPIGMAMNKN LTMKMGNCNH RKYIPKLLEL
VRTGVVDPTA ILSHVEPMGS AIDAYRNFDA RKPGWVKVEL EPTQLQ
//
