ID A0A0A2E918_9PORP Unreviewed; 568 AA.
AC A0A0A2E918;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KGN72949.1};
GN ORFNames=HQ47_08795 {ECO:0000313|EMBL:KGN72949.1};
OS Porphyromonas macacae.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=28115 {ECO:0000313|EMBL:KGN72949.1, ECO:0000313|Proteomes:UP000030103};
RN [1] {ECO:0000313|EMBL:KGN72949.1, ECO:0000313|Proteomes:UP000030103}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COT-192 OH2859 {ECO:0000313|Proteomes:UP000030103};
RA Wallis C., Deusch O., O'Flynn C., Davis I., Horsfall A., Kirkwood N.,
RA Harris S., Eisen J.A., Coil D.A., Darling A.E., Jospin G., Alexiev A.;
RT "Draft Genome Sequence of Porphyromonas macacae COT-192_OH2859.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGN72949.1}.
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DR EMBL; JRFA01000025; KGN72949.1; -; Genomic_DNA.
DR RefSeq; WP_036874832.1; NZ_JRFA01000025.1.
DR AlphaFoldDB; A0A0A2E918; -.
DR STRING; 28115.HQ47_08795; -.
DR eggNOG; COG1960; Bacteria.
DR OrthoDB; 9802867at2; -.
DR Proteomes; UP000030103; Unassembled WGS sequence.
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; 1.20.120.470; Acyl-CoA dehydrogenase, C-terminal domain; 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; IPR020964; Acyl-CoA_dehydrogenase_C.
DR InterPro; IPR036797; Acyl-CoA_dehydrogenase_C_sf.
DR InterPro; IPR006089; Acyl-CoA_DH_CS.
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; PTHR42803; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR42803:SF1; BROAD-SPECIFICITY LINEAR ACYL-COA DEHYDROGENASE FADE5; 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 Pfam; PF12186; AcylCoA_dehyd_C; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR SUPFAM; SSF158494; PG0775 C-terminal domain-like; 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|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000030103}.
FT DOMAIN 52..169
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 173..268
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 283..444
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 452..562
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12186"
SQ SEQUENCE 568 AA; 64494 MW; CD49D073625F00ED CRC64;
MANFYTDTPE LRFHLNDPLM KRIVELKERN FADKDQYDYA PVDFEDAMDS YERVLQEVGD
ICANIIAPNA EQVDLDGCHV ENKRAVLPKG TIENLEATKK AGLNGISMPR RLGGLNFPIV
PYMMAADIVS RSDAGFENLW GLQDCAETIY EFGSEEQKQK YITRACNGDT MSMDLTEPDA
GSDLQAVMLK ATYNEEEDCW YLNGVKRFIT NGDSDIHLVL ARSEEGTHDG RGLSMFIYDK
RNGGVDVRRI ENKMGIKGVP ACELTFKNAK AELVGSRKLG LIKYVMALMN GARLGISAQS
VGISQAAYNE ALSYARERRQ FGKAIIDIPA VAEMLTNIKT KLDASRALLY ETSRYVDMYK
VLDDIAKERK LTPEERAENK KYAKWVDSFT PLAKGIGSEF ANQNVYDCVQ VHGGSGFMKD
YACERLHRDV RITSIYEGTT QLQVVAAIRY VTNGTYLEIM KEMEQNEVKP EMQNLMVRLH
KLAERYALAV TQITEKKDQE LLDFMSRRLV EMAAYTLMGH LLVRDASRDS MFDKSANVFV
RYAEGEFDKH IGFIEQFNDE DMAYYRHN
//
