ID F9WYR2_ZYMTI Unreviewed; 512 AA.
AC F9WYR2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Cytochrome b5 heme-binding domain-containing protein {ECO:0000259|PROSITE:PS50255};
GN ORFNames=MYCGRDRAFT_65057 {ECO:0000313|EMBL:EGP92702.1};
OS Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch
OS fungus) (Septoria tritici).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=336722 {ECO:0000313|EMBL:EGP92702.1, ECO:0000313|Proteomes:UP000008062};
RN [1] {ECO:0000313|EMBL:EGP92702.1, ECO:0000313|Proteomes:UP000008062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115943 / IPO323 {ECO:0000313|Proteomes:UP000008062};
RX PubMed=21695235; DOI=10.1371/journal.pgen.1002070;
RA Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J., Crane C.F.,
RA Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J., Aerts A.,
RA Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J., van der Burgt A.,
RA Canto-Canche B., Churchill A.C.L., Conde-Ferraez L., Cools H.J.,
RA Coutinho P.M., Csukai M., Dehal P., De Wit P., Donzelli B.,
RA van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E., Henrissat B.,
RA Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y., Kuzniar A.,
RA Lindquist E., Lombard V., Maliepaard C., Martins N., Mehrabi R.,
RA Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A., Schmutz J.,
RA Schouten H.J., Shapiro H., Stergiopoulos I., Torriani S.F.F., Tu H.,
RA de Vries R.P., Waalwijk C., Ware S.B., Wiebenga A., Zwiers L.-H.,
RA Oliver R.P., Grigoriev I.V., Kema G.H.J.;
RT "Finished genome of the fungal wheat pathogen Mycosphaerella graminicola
RT reveals dispensome structure, chromosome plasticity, and stealth
RT pathogenesis.";
RL PLoS Genet. 7:E1002070-E1002070(2011).
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; CM001196; EGP92702.1; -; Genomic_DNA.
DR RefSeq; XP_003857726.1; XM_003857678.1.
DR AlphaFoldDB; F9WYR2; -.
DR STRING; 336722.F9WYR2; -.
DR EnsemblFungi; Mycgr3T65057; Mycgr3P65057; Mycgr3G65057.
DR GeneID; 13403297; -.
DR KEGG; ztr:MYCGRDRAFT_65057; -.
DR VEuPathDB; FungiDB:ZTRI_1.197; -.
DR eggNOG; KOG0141; Eukaryota.
DR eggNOG; KOG0537; Eukaryota.
DR HOGENOM; CLU_018204_4_4_1; -.
DR InParanoid; F9WYR2; -.
DR OMA; EQPVMRQ; -.
DR OrthoDB; 294001at2759; -.
DR Proteomes; UP000008062; Chromosome 1.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
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 InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR018506; Cyt_B5_heme-BS.
DR PANTHER; PTHR48083:SF28; ACYL-COA DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10880); 1.
DR PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED; 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; PF00173; Cyt-b5; 1.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008062}.
FT DOMAIN 2..77
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
SQ SEQUENCE 512 AA; 57582 MW; 152F045B223E38AF CRC64;
MSAPLTRQEV QKHTSEEDLW VIVDHVVYDL SDFVDAHPGG SVVLRQVAGQ DATEAFYNLH
RQEVLQQYKS LAIGVLEGEK PEVISPQPGD LSQVPYGEPL WLNSQFKSPY YNESHRRLQK
ACRAFCEKEI MPEAKEKEMS GEYISQELIN KMAETNLLAC RLGPGKHLHG RNIFDGAVKG
DEYDYFHDMI VSQEIARVSQ RGFQDGNMAG MTISLTAVHQ WLKDDELRER VSKEVLSGQK
KICLAVTEAF AGSDVAGLRT TCEESEDGQH YIVNGTKKWI TNGMWCDYFV TGCKTDKGFT
VLLIPRGEGV ETKPIKTSYS PAAATSYIEF DNVKVPKRNI LGPEHKGFVV IMSNFNHERY
MMCAMVARWS RTVVEECLKW SHQRMVFGQP LISQPVIRQK LAKMISHVEA NQAWIENITY
QMCNMSYDEQ SKNLSGPIGL LKVFCTRSAH EVADDAVGVF GGRALTQTGM GRVIEMFNRT
NKFDAVLGGT EEILADLGVR QAMKFMPKGA KL
//
