ID A0A395HBI9_9EURO Unreviewed; 1155 AA.
AC A0A395HBI9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:RAL05301.1};
GN ORFNames=BO80DRAFT_478295 {ECO:0000313|EMBL:RAL05301.1};
OS Aspergillus ibericus CBS 121593.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448316 {ECO:0000313|EMBL:RAL05301.1, ECO:0000313|Proteomes:UP000249402};
RN [1] {ECO:0000313|EMBL:RAL05301.1, ECO:0000313|Proteomes:UP000249402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121593 {ECO:0000313|EMBL:RAL05301.1,
RC ECO:0000313|Proteomes:UP000249402};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KZ824421; RAL05301.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395HBI9; -.
DR STRING; 1448316.A0A395HBI9; -.
DR VEuPathDB; FungiDB:BO80DRAFT_478295; -.
DR OrthoDB; 4517707at2759; -.
DR Proteomes; UP000249402; Unassembled WGS sequence.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:InterPro.
DR CDD; cd00302; cytochrome_P450; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 2.
DR InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd.
DR InterPro; IPR006108; 3HC_DH_C.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR InterPro; IPR000033; LDLR_classB_rpt.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR48075; 3-HYDROXYACYL-COA DEHYDROGENASE FAMILY PROTEIN; 1.
DR PANTHER; PTHR48075:SF10; DEHYDROGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G10070)-RELATED; 1.
DR Pfam; PF00725; 3HCDH; 1.
DR Pfam; PF02737; 3HCDH_N; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SMART; SM00135; LY; 4.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF63825; YWTD domain; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000249402}.
FT DOMAIN 554..716
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 730..820
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 1155 AA; 128348 MW; 3F1F4818B260134C CRC64;
MSNQQFYLLG ESVASAKDIT IEATLDLDQL KQLVAAYFAI VDPSGIGFQT ENDCLSDVSD
VLAAKGPVAI SIDGHAVREP GGPRGLPFVG NHFEVYPDHL GNHQRLFDQY GPIFKTTNLG
RTTYQTNDPQ ISAIVFAESD FFSKIISDAH PLSALKTPSA GVFLGDTDTP EWKAAHKFLP
PALGPKAVRH YAPTMQRAVE DSFRVFDALD EQEEAWNVYQ YMLKLGSQAV GELTLGIDFK
HFTSPDAPVH EMVHSIAEML SLNKKVTSKG DWYGMLPFGD PQRLRNLKAR IEEMVDESIQ
NAERAGISDL PLQDAALLSS NMVDYALRAT DNKGEKLPKS SLVWALVVAT AAGFTTTSSL
LSWLIYGLVT YPGMQERLLQ ELVDNDITED TELTAELTEK LLFQDKYIKE MQRRHNPSFQ
PGRTAKVDLV LPGGYKIPKD AVIIPALHHI HNNPNLWDNP TRFNPDRWDT PEVKARHKAA
YIPFAMGPRM CIGFNFALQE IKVFLPKLIY RYHFSREGNG PIEYDPMFQL IRPNNLLTMR
PTWSPPHDYQ NRPVAVLGAG VLGRRIGCIW ASAGYTVHLR DPNPDQLSAG IAYIQENVAA
YATKTGRSPG TAHSFTDLKE AVSTAWLIIE AVPEKLPLKI TTFAELSTLA PTDSILASNS
SSYKTSEMLE RVPETVKSRI LNMHYYMPPQ CMLVELMTDG FTCEDIFPFL VERCREGATS
PYVARKESTG FIFNRLWAAV KREVLTILSE GVSVPKEIDA MWEEMFITGR VKPCEMMDNV
GLDTVAFIEQ HYIHERGLPA DKTVDYLTAN YLDHGKLGSK CPLGGLYPPA ITNNNTSINS
NKRLLILDIG LASSTAATSI STPAGHILSL TPTPTFTPNN TQLQTILSNQ LLPDGITYSR
TTNRIYWTCM GIPAHPDGAI YSSTLDGKDI RSLLPKGTLN TPKQITLDPT TQKLYFCDRE
GCAVYRCNLD GTDLTCLVSR HNPKETAENG TPTSNARNWC VGIAVSPRWN KFYWTQKGAS
KSGQGRIFCA SLDTAHPIEG EEGGQCILDG LPEPIDLEVD EARGELYWTD RGELPLGNSL
NRVKLDAEGV PVRGAKVEVL VRNLKEAIGV CCDRETGDFY LTDLGGCVYR WNRDRREKVR
LYEEEGRAFT GIVCV
//
