ID Q0U898_PHANO Unreviewed; 471 AA.
AC Q0U898;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 2.
DT 27-MAR-2024, entry version 101.
DE RecName: Full=Cytochrome b5 heme-binding domain-containing protein {ECO:0000259|PROSITE:PS50255};
GN ORFNames=SNOG_12016 {ECO:0000313|EMBL:EAT80428.2};
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT80428.2, ECO:0000313|Proteomes:UP000001055};
RN [1] {ECO:0000313|Proteomes:UP000001055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC {ECO:0000313|Proteomes:UP000001055};
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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}.
CC -!- SIMILARITY: Belongs to the cytochrome b5 family.
CC {ECO:0000256|RuleBase:RU362121}.
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DR EMBL; CH445345; EAT80428.2; -; Genomic_DNA.
DR RefSeq; XP_001802248.1; XM_001802196.1.
DR AlphaFoldDB; Q0U898; -.
DR STRING; 321614.Q0U898; -.
DR EnsemblFungi; SNOT_12016; SNOT_12016; SNOG_12016.
DR GeneID; 5979158; -.
DR KEGG; pno:SNOG_12016; -.
DR VEuPathDB; FungiDB:JI435_120160; -.
DR eggNOG; KOG0137; Eukaryota.
DR eggNOG; KOG0537; Eukaryota.
DR HOGENOM; CLU_018204_4_3_1; -.
DR InParanoid; Q0U898; -.
DR OrthoDB; 294001at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IBA:GO_Central.
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; 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, ECO:0000256|RuleBase:RU362121};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU362121};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU362121};
KW Reference proteome {ECO:0000313|Proteomes:UP000001055}.
FT DOMAIN 3..78
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
SQ SEQUENCE 471 AA; 52689 MW; 096F4AD78C67BBCE CRC64;
MSQETLTRES VAKHNKPDDL WCIVDHKVYD LTDFVDAHPG GSVVLEQVAG TDATIAFYNL
HRQEVLQKYE DLCIGTIEGE KSEVIVPKFG DLSPVPYAEP LWLRPQFKSP YFKESHRALQ
KELRKFTDEH ITPEAQAKEK SGEYISQELI DKMAANDILA MRLGPGKHLH GKNLMGVVKG
EEFDYLHDLV QAQEGVRANA RGFQDGNMAG MMISLTAVLQ WMPESELKTR VVNEVLTGQK
KICLAITEAF AGSDVAGLRT TAEKTPDGKH YIIRGTKKWI TNGMFCDYFV TGCKTESGFS
VILIPRDDTV ETKLIKTSYS TAAGTAYVEF NNTKVPVEGL LGKEHQGFIV ISKSNSTPSH
LTTSNNTSVS NFNHERFMMA CGVIRQSRTV VEECLKWCNQ RMVFGKKLIE QARHPPKTRQ
NDLSRRGQPG VARIHRLPNV QHELPAAVNC AGWAHWALEV FCHALCARDC G
//
