ID A0A0J8QZJ7_COCIT Unreviewed; 429 AA.
AC A0A0J8QZJ7;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 08-NOV-2023, entry version 22.
DE SubName: Full=Glutaryl-CoA dehydrogenase {ECO:0000313|EMBL:KMU76818.1};
GN ORFNames=CISG_05651 {ECO:0000313|EMBL:KMU76818.1};
OS Coccidioides immitis RMSCC 3703.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=454286 {ECO:0000313|EMBL:KMU76818.1, ECO:0000313|Proteomes:UP000054559};
RN [1] {ECO:0000313|Proteomes:UP000054559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RMSCC 3703 {ECO:0000313|Proteomes:UP000054559};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(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; DS268149; KMU76818.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J8QZJ7; -.
DR STRING; 454286.A0A0J8QZJ7; -.
DR Proteomes; UP000054559; Unassembled WGS sequence.
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; cd01151; GCD; 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; PTHR42807; GLUTARYL-COA DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR42807:SF1; GLUTARYL-COA DEHYDROGENASE, MITOCHONDRIAL; 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; 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:UP000054559}.
FT DOMAIN 49..160
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 164..262
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 281..422
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 429 AA; 46489 MW; 40BEF278B3E38E94 CRC64;
MNTSLLGRTA RGALNVTKAT SSSLSRRCAS SSAARFDWQD PLNAANLYTP EELAIAETAR
QYCQERLMPR VLESYRNEDY DKTMLQEMGE LGLLGATIEG YGCAGVSTVA SGLITKEVER
VDSGFRSGMS VQSSLIMTGI HEFGTKELKE KYLPGLAKGK LIGCFGLTEP NHGSDPGSME
TVARSHPTKK GYYSLTGAKT WITNSPISDL FLVWAKLEST GKIKGFIVQR DQCPPGTLET
PAIKNKTALR ASITGMIQLD NCPVPEENML PDVEGLVGPF TCLNSARLGI AFGTMGALED
CIDRARTYSL ERKQFKGNPL AKYQLIQKKL ADAATDAAYG TLAAVQVARL KDEGKCTPEM
ISMTKRQNCD RALVGARTLQ EVFGGNAASD EYHIGRHVAN LFVAQTYEGQ SDIHSLILGR
AITGVQAFC
//
