ID C5ZYT5_9HELI Unreviewed; 377 AA.
AC C5ZYT5;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Putative acyl-CoA dehydrogenase {ECO:0000313|EMBL:EES89193.1};
GN Name=fadE16 {ECO:0000313|EMBL:EES89193.1};
GN ORFNames=HCAN_0476 {ECO:0000313|EMBL:EES89193.1};
OS Helicobacter canadensis MIT 98-5491.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=537970 {ECO:0000313|EMBL:EES89193.1, ECO:0000313|Proteomes:UP000007032};
RN [1] {ECO:0000313|EMBL:EES89193.1, ECO:0000313|Proteomes:UP000007032}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 13241 {ECO:0000313|Proteomes:UP000007032};
RX PubMed=19542273; DOI=10.1128/JB.00729-09;
RA Loman N.J., Snyder L.A., Linton J.D., Langdon R., Lawson A.J.,
RA Weinstock G.M., Wren B.W., Pallen M.J.;
RT "Genome sequence of the emerging pathogen Helicobacter canadensis.";
RL J. Bacteriol. 191:5566-5567(2009).
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; CM000776; EES89193.1; -; Genomic_DNA.
DR RefSeq; WP_006655169.1; NZ_DS990368.1.
DR AlphaFoldDB; C5ZYT5; -.
DR STRING; 537970.HCAN_0476; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_3_2_7; -.
DR OrthoDB; 9765339at2; -.
DR Proteomes; UP000007032; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR CDD; cd00567; ACAD; 1.
DR Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR PANTHER; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43884:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR PIRSF; PIRSF016578; HsaA; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 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:UP000007032}.
FT DOMAIN 4..112
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 116..210
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 240..359
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 377 AA; 41678 MW; 3B06F34ADF9C5E52 CRC64;
MPTLENLEEK IQKLGEQFIL PYTKEIDQEA RFPKEAYEAL KQQGFMGLLV PKEYGGLQGN
NLDHAEVCYN LARFNASTAL CYMMHNVATA CVSHYGTAHQ KSLYLPKIAK GEATFALAYS
ESGSGTHFVN PDITESQKGE KRILEGRKSF VTSAQQANYY LTYTNSCKLQ GKKNNWIVPS
DHPSLTHEEG VWNGFGMRGN VSKPVQYNQV ELEVADCLLG SEGDGENQIN LVAMYFVTGL
GAVYSGVGMA AYECALQHCL TRKYSDGKDL ADNELVRIHL AELYTKTQSQ IALVREAARA
FDSGASDAPM KIFACRINTT HLVMEICELA MRLGGGKAYS KHLPLEQYLR DAMASQVMAP
SLDVLKIWLG NAITNKG
//
