ID C7QHP2_CATAD Unreviewed; 725 AA.
AC C7QHP2;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Acyl-CoA dehydrogenase domain protein {ECO:0000313|EMBL:ACU71067.1};
GN OrderedLocusNames=Caci_2148 {ECO:0000313|EMBL:ACU71067.1};
OS Catenulispora acidiphila (strain DSM 44928 / JCM 14897 / NBRC 102108 / NRRL
OS B-24433 / ID139908).
OC Bacteria; Actinomycetota; Actinomycetes; Catenulisporales;
OC Catenulisporaceae; Catenulispora.
OX NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU71067.1, ECO:0000313|Proteomes:UP000000851};
RN [1] {ECO:0000313|EMBL:ACU71067.1, ECO:0000313|Proteomes:UP000000851}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44928 / JCM 14897 / NBRC 102108 / NRRL B-24433 / ID139908
RC {ECO:0000313|Proteomes:UP000000851};
RX PubMed=21304647; DOI=10.4056/sigs.17259;
RA Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S., Chen F.,
RA Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Mikhailova N.,
RA Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Chain P.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Ali Z., Tindall B.J., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT 139908).";
RL Stand. Genomic Sci. 1:119-125(2009).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347}.
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DR EMBL; CP001700; ACU71067.1; -; Genomic_DNA.
DR AlphaFoldDB; C7QHP2; -.
DR STRING; 479433.Caci_2148; -.
DR KEGG; cai:Caci_2148; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_9_3_11; -.
DR InParanoid; C7QHP2; -.
DR Proteomes; UP000000851; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 2.
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; 2.
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; PTHR43292; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43292:SF4; ACYL-COA DEHYDROGENASE FADE34; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 2.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 2.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 2.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000000851}.
FT DOMAIN 218..351
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 385..465
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 469..561
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 576..720
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 725 AA; 76330 MW; FDE5CED144E4D7AE CRC64;
MTAGIGSIGI TSEHRDLAEA VRGWLARAVP PAAVRAALDA EQEERPAFWG DLAKQGLLYG
DELDGLLPLA VTLEETGRAA TPGPFLPTVT AAVFLQAAGG SGSADILAAL ADGSATAAVA
SHAGTVVAEP IEGGYLLVGE VEPVIGAALA DWLLLTARRS DGSEIQALVP AADVVISPLV
SLDRTRRVAK AGVERVFVPR AQVIVAATAL LDRIAALLAS AEAVGIADWC TRTAAEYAKV
RVQFGKPIGQ FQGVKHRCAA MVARMEQARS AVWDAAYVAG SGIAGEDAEV PVAIAAALAL
EAAVECAKDC IQVLGGIGFT WEHDAHVYLR RALTLRQMYG PSSRWRARVA ELTAAGRRRE
LKVELPEEAD AYREAAREAF AGVRELTPAE QRKALAVTGY AAPYLTKPYG LSAGPVEQIV
IAQEMAAAKV RLPDIIIGNW VVPTLVKYGS DEQRERFVLP TLRGEVIWCQ LFSEPGAGSD
LAALTTRATR VAGGWRLDGQ KVWTSVANFA QWAICIARTS PDKPKHEGIT YFLVDMKSDG
VDVRPLREIT GASMFNEVFL DGVFVPDELV VGEVDGGWPL ARNTLGNERV SLASGPVLGG
SLEGLLTSVA ARSELDPVLA DRLGELVCQG QSAALLGLRT TLRQLSGMEQ GPEASIRKLI
SMKLAQDVAE LGLELLGGAG ATEAGGAAAG WTQAFLSSRC LTIAGGTTEV QLNVIGERIL
GLPRD
//
