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Database: UniProt
Entry: A7MM85_CROS8
LinkDB: A7MM85_CROS8
Original site: A7MM85_CROS8 
ID   A7MM85_CROS8            Unreviewed;       544 AA.
AC   A7MM85;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, sequence version 1.
DT   24-JAN-2024, entry version 89.
DE   RecName: Full=Isovaleryl-CoA dehydrogenase {ECO:0008006|Google:ProtNLM};
GN   OrderedLocusNames=ESA_00194 {ECO:0000313|EMBL:ABU75495.1};
OS   Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Cronobacter.
OX   NCBI_TaxID=290339 {ECO:0000313|EMBL:ABU75495.1, ECO:0000313|Proteomes:UP000000260};
RN   [1] {ECO:0000313|EMBL:ABU75495.1, ECO:0000313|Proteomes:UP000000260}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-894 {ECO:0000313|EMBL:ABU75495.1,
RC   ECO:0000313|Proteomes:UP000000260};
RX   PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA   Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA   Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA   Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA   McClelland M., Forsythe S.J.;
RT   "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT   hybridization analysis with other Cronobacter species.";
RL   PLoS ONE 5:E9556-E9556(2010).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU362125};
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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DR   EMBL; CP000783; ABU75495.1; -; Genomic_DNA.
DR   RefSeq; WP_012123694.1; NC_009778.1.
DR   AlphaFoldDB; A7MM85; -.
DR   KEGG; esa:ESA_00194; -.
DR   PATRIC; fig|290339.8.peg.172; -.
DR   HOGENOM; CLU_016513_0_0_6; -.
DR   OMA; GNVQCLD; -.
DR   Proteomes; UP000000260; Chromosome.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.40.110.20; -; 1.
DR   Gene3D; 6.10.250.600; -; 1.
DR   Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR   InterPro; IPR006089; Acyl-CoA_DH_CS.
DR   InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR   InterPro; IPR036250; AcylCo_DH-like_C.
DR   InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR   InterPro; IPR041504; AidB_N.
DR   PANTHER; PTHR42707; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR42707:SF3; ACYL-COA DEHYDROGENASE AIDB-RELATED; 1.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF18158; AidB_N; 1.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR   PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR   PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362125};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU362125};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000260}.
FT   DOMAIN          10..167
FT                   /note="Adaptive response protein AidB N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18158"
FT   DOMAIN          181..278
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          289..443
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   544 AA;  60101 MW;  D40BDD14F098C3C3 CRC64;
     MHWQTHTVFN QPVALNNSNL YLSDTALREA VLREGAGWDA ELLASIGQQL GTAESLELGR
     LANANPPELL RYDARGERLD DVRFHPAWHL LMQGLFANRV HNLPWLETAR EGALVARAAR
     FVLHAQVEAG TLCPITMTFA ATPLLQAHLP PLFADWQTPL ASDRYDSHLL PGAQKRGLLI
     GMGMTEKQGG SDVLSNTTRA EPVAGRGPGE AYRLVGHKWF FSVPQSDAHL VLAQTKGGLS
     CFFVPRFLPD GQRNAVRLER LKDKLGNRSN ASSEAEFLDA LGWLLGEEGE GVRQILRMGG
     MTRFDCALGS HGLMRRALAV ALYHTHQRQA FGKNLIDQPL MRQVLGRMAL ELEGQTALLF
     RLARAWEQRE SPHEVAFARL FTPAAKYGVC KRGIPFVAEA MEALGGIGYC EESELPRLYR
     EMPVNSIWEG SGNIMCLDVL RVLTRQPGVL EMLSHEFDAV KGQDRHFDRA WRQLAGQLRR
     PDEAAGRAIT TQLFLLASGA QVLRSLTPPL AQAWCRMMLD TRGDSPLPEP VLAQALLRAT
     GGAG
//
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