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
//