ID C8WWK6_ALIAD Unreviewed; 582 AA.
AC C8WWK6;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 24-JAN-2024, entry version 66.
DE SubName: Full=Acyl-CoA dehydrogenase domain protein {ECO:0000313|EMBL:ACV58477.1};
GN OrderedLocusNames=Aaci_1452 {ECO:0000313|EMBL:ACV58477.1};
OS Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC 27009 /
OS DSM 446 / BCRC 14685 / JCM 5260 / KCTC 1825 / NBRC 15652 / NCIMB 11725 /
OS NRRL B-14509 / 104-IA) (Bacillus acidocaldarius).
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Alicyclobacillus.
OX NCBI_TaxID=521098 {ECO:0000313|EMBL:ACV58477.1, ECO:0000313|Proteomes:UP000001917};
RN [1] {ECO:0000313|Proteomes:UP000001917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27009 / DSM 446 / BCRC 14685 / JCM 5260 / KCTC 1825 / NBRC
RC 15652 / NCIMB 11725 / NRRL B-14509 / 104-IA
RC {ECO:0000313|Proteomes:UP000001917};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Ovchinnikova G., Chertkov O., Sims D., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Pukall R., Klenk H.-P., Eisen J.A.;
RT "The complete chromosome of Alicyclobacillus acidocaldarius subsp.
RT acidocaldarius DSM 446.";
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACV58477.1, ECO:0000313|Proteomes:UP000001917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27009 / DSM 446 / BCRC 14685 / JCM 5260 / KCTC 1825 / NBRC
RC 15652 / NCIMB 11725 / NRRL B-14509 / 104-IA
RC {ECO:0000313|Proteomes:UP000001917};
RX PubMed=21304673; DOI=10.4056/sigs.591104;
RA Mavromatis K., Sikorski J., Lapidus A., Glavina Del Rio T., Copeland A.,
RA Tice H., Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L.,
RA Pitluck S., Ivanova N., Ovchinnikova G., Pati A., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Meincke L.,
RA Sims D., Chertkov O., Han C., Brettin T., Detter J.C., Wahrenburg C.,
RA Rohde M., Pukall R., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Alicyclobacillus acidocaldarius type strain
RT (104-IA).";
RL Stand. Genomic Sci. 2:9-18(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; CP001727; ACV58477.1; -; Genomic_DNA.
DR AlphaFoldDB; C8WWK6; -.
DR STRING; 521098.Aaci_1452; -.
DR KEGG; aac:Aaci_1452; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_3_3_9; -.
DR OMA; FGYTRLM; -.
DR Proteomes; UP000001917; 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; 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; 2.
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; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43884:SF38; ACYL-COA DEHYDROGENASE-RELATED; 1.
DR Pfam; PF21343; ACAD9-ACADV_C; 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 SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 2.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM 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|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000001917}.
FT DOMAIN 25..137
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 141..234
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 246..419
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 582 AA; 62802 MW; 54D3CB2835926D2F CRC64;
MRRTVDVIQE FHPGLKDALT PERRSDEHNL IEETARSFVE RDVLPRMEAL EAGDVNVLKA
LYRKAGELGL IGVDLPEAYG GLELDPLSSL LVSETLGETA GFGVSINIHS GVALHPILYF
GDEAQRAVYL PQLAAGEVIA SYALTEPDAG SDALHGKTSA RRDEARGCYV LSGQKQWISN
ARVAGVYVVF AQLANRGMTA FVVDRDRPGV SVGKEEHKVG IHASPTASLI LDDVEVPESA
LLGAPGHGHR IALSVLNLAR HKMALYALGQ TRRAIRIAAA YAKERRQFGV PIASFGMIRE
KLGYMAARYF VARSAAYRTA GELAPGKKRA LDLALRPDLE PEEKVRGVAS ALSSCIAACS
LNKVLATEVQ AFVIDEAVQI HGGYGYMEDY EIARMYRDAR ITRIFEGTNE INRLAAVRDL
LSSRAREASA CSLSDPSSPA ASPSLAAHLP AGRLRSTLEG AEQALRAMKT GFDAVVEAAL
AREGARLADQ QALVRRLADA KMWLYAFESA LVRVALAADA RGPARDLGAE LAAVAWADAV
RHGFTPLLEA ARHVGVKLDG LDYPDEIGQL QAIAEYVLDR VR
//