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Database: UniProt
Entry: I1C4D1_RHIO9
LinkDB: I1C4D1_RHIO9
Original site: I1C4D1_RHIO9 
ID   I1C4D1_RHIO9            Unreviewed;       920 AA.
AC   I1C4D1;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=Cytochrome b5 heme-binding domain-containing protein {ECO:0000259|PROSITE:PS50255};
GN   ORFNames=RO3G_08016 {ECO:0000313|EMBL:EIE83311.1};
OS   Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL
OS   43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX   NCBI_TaxID=246409 {ECO:0000313|EMBL:EIE83311.1, ECO:0000313|Proteomes:UP000009138};
RN   [1] {ECO:0000313|EMBL:EIE83311.1, ECO:0000313|Proteomes:UP000009138}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880
RC   {ECO:0000313|Proteomes:UP000009138};
RX   PubMed=19578406; DOI=10.1371/journal.pgen.1000549;
RA   Ma L.-J., Ibrahim A.S., Skory C., Grabherr M.G., Burger G., Butler M.,
RA   Elias M., Idnurm A., Lang B.F., Sone T., Abe A., Calvo S.E.,
RA   Corrochano L.M., Engels R., Fu J., Hansberg W., Kim J.-M., Kodira C.D.,
RA   Koehrsen M.J., Liu B., Miranda-Saavedra D., O'Leary S.,
RA   Ortiz-Castellanos L., Poulter R., Rodriguez-Romero J., Ruiz-Herrera J.,
RA   Shen Y.-Q., Zeng Q., Galagan J., Birren B.W., Cuomo C.A., Wickes B.L.;
RT   "Genomic analysis of the basal lineage fungus Rhizopus oryzae reveals a
RT   whole-genome duplication.";
RL   PLoS Genet. 5:E1000549-E1000549(2009).
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; CH476737; EIE83311.1; -; Genomic_DNA.
DR   AlphaFoldDB; I1C4D1; -.
DR   STRING; 246409.I1C4D1; -.
DR   VEuPathDB; FungiDB:RO3G_08016; -.
DR   eggNOG; KOG0139; Eukaryota.
DR   eggNOG; KOG0537; Eukaryota.
DR   eggNOG; KOG1182; Eukaryota.
DR   InParanoid; I1C4D1; -.
DR   OrthoDB; 1474114at2759; -.
DR   Proteomes; UP000009138; Unassembled WGS sequence.
DR   GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity; IEA:UniProtKB-EC.
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   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR   CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR   Gene3D; 3.40.50.970; -; 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   Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 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   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   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR029061; THDP-binding.
DR   PANTHER; PTHR43380; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43380:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT ALPHA, 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   Pfam; PF00173; Cyt-b5; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   PRINTS; PR00363; CYTOCHROMEB5.
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   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009138}.
FT   DOMAIN          2..78
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
SQ   SEQUENCE   920 AA;  103596 MW;  A7C0AF9473967920 CRC64;
     MSKKFTIEEV AKHTQADDCW IIVHDKVYDI SKFLDDHPGG KKVLLKAAGT DATKQFEAFH
     NPSVLTKVAA QYLIGDIGAE VEDDDDIPNA NPLQVGESYG DMVPFGDPMW YQDWYSPYYD
     DSHRKVRKSV RDFVEREIMP YTHEWDEAKE LPREVYIKAA KAGLLASVVG HVEAEYIPYD
     LPGNIKHEDF DAFHSLIVTD EISRCASGGV TWGLMGGLGI GLPPIIHFGS RYLKNKVIRD
     CLSGEKHICL AITEPTGGSD VANLQTEAKD MGDHYLVNGE KKWITNGTFA DYFTVACRTG
     EPGFNGLSFL LIERGMPGVI TRQMKCSGVW PSGTAYITFE DVKVPKENLI GKENKGFKYI
     MQNFNSERIG IVIQANRFAR CCVEEALKYA HKRKTFGKRL VDHPVIRNKF ANMIRKVEAT
     HAWLEILVYQ AKNMPTELQP IRLGGPIALC KAQSTRTFEF CAREAAQIFG GLAYTRGGQG
     EKVERLYREV RAFAIPGGSE EIMLDLGVRQ ALFNNASVNV AEVANDGQNK STWSSADKFM
     NEMKFIQQIE PLKAYRVMDH TGTVLNPEHD PNLSKEEVTK CYKSMLLLHT MDGILYDAQR
     QGRISFYMTH YGEEAMIGSA AALLPEDVVF GQYREAFMLV YRGFTLDEFV NQCFSNELDY
     GKGRQMPIHY GSKRLNFQTI SSPLGTQIPQ ASGAAYALKR SGANACTLCF FGEGAASEGD
     FHAGLNMAAT LKCPVIFFCR NNGFAISTPS SEQYKGDGIA SRGIGYGIDT IRVDGNDIWA
     IYNATKVARE IAVKEQRPVL IEAMTYRIGH HSTSDDSTKY RDRKEVEERA QLDNPITRLK
     KYMEAKGWWS AQEEEDYRKK VKKEILASFS AAEKKKKPAL KHLFTDVYDE MTPNLVRQQN
     ELNELIQKYP EYYNTDEFAS
//
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