ID A1DAD5_NEOFI Unreviewed; 427 AA.
AC A1DAD5;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Thermophilic desulfurizing enzyme family protein {ECO:0000313|EMBL:EAW19825.1};
GN ORFNames=NFIA_094450 {ECO:0000313|EMBL:EAW19825.1};
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW19825.1, ECO:0000313|Proteomes:UP000006702};
RN [1] {ECO:0000313|Proteomes:UP000006702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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DR EMBL; DS027694; EAW19825.1; -; Genomic_DNA.
DR RefSeq; XP_001261722.1; XM_001261721.1.
DR AlphaFoldDB; A1DAD5; -.
DR STRING; 331117.A1DAD5; -.
DR EnsemblFungi; EAW19825; EAW19825; NFIA_094450.
DR GeneID; 4588903; -.
DR KEGG; nfi:NFIA_094450; -.
DR VEuPathDB; FungiDB:NFIA_094450; -.
DR eggNOG; ENOG502S9JP; Eukaryota.
DR HOGENOM; CLU_018204_10_1_1; -.
DR OMA; HNWDNVG; -.
DR OrthoDB; 2264654at2759; -.
DR Proteomes; UP000006702; Unassembled WGS sequence.
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; 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; IPR013107; Acyl-CoA_DH_C.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_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; PF08028; Acyl-CoA_dh_2; 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 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000006702}.
FT DOMAIN 34..127
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 260..401
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08028"
SQ SEQUENCE 427 AA; 47059 MW; 2F6B22BD086ABA44 CRC64;
MAQANVPATD PAVYDAYKEK WAALPDSADA WLARAREVAE VLAQDAAQRD QDNKSPRAEV
VLLKHSGLLK LLGPKKYGGG EQPWRVGYKA IREVAKGDGS IGMLLGYHLL WSTTANVVGT
AEQADRLQEL IITNNLFVGG AVNPRDNDLK ITSDGDSIVF NGFKHFNTGG VVSDLTVLEG
VLDGTQDHIF AVVETNQSGI QFAHNWKNIG LRLTESGSVK IENVRASWTD ALGWDATTKR
PLAEILTIPF ASLFLPTIQL VFSNFYLGIA IGALEFAAKY TTTSTRAWPY GGDNKEAATD
EFYILERYGN FFAHLRAAEA LADKAGDQLS ALYERHSGDR LKVTAEERGE VAEWVASVKV
VTTDVGLRVT SGIFEVTGAR ATSLKVGLDR FWRDIRTHTL HDPVAYKNRE LGRYVLLHEY
PEPTWYT
//
