ID A0A3N4J1E1_9PEZI Unreviewed; 1157 AA.
AC A0A3N4J1E1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Molybdenum cofactor-binding domain-containing protein {ECO:0000313|EMBL:RPA90391.1};
GN ORFNames=L873DRAFT_1831724 {ECO:0000313|EMBL:RPA90391.1};
OS Choiromyces venosus 120613-1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Tuberaceae; Choiromyces.
OX NCBI_TaxID=1336337 {ECO:0000313|EMBL:RPA90391.1, ECO:0000313|Proteomes:UP000276215};
RN [1] {ECO:0000313|EMBL:RPA90391.1, ECO:0000313|Proteomes:UP000276215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=120613-1 {ECO:0000313|EMBL:RPA90391.1,
RC ECO:0000313|Proteomes:UP000276215};
RX PubMed=30420746; DOI=10.1038/s41559-018-0710-4;
RA Murat C., Payen T., Noel B., Kuo A., Morin E., Chen J., Kohler A.,
RA Krizsan K., Balestrini R., Da Silva C., Montanini B., Hainaut M.,
RA Levati E., Barry K.W., Belfiori B., Cichocki N., Clum A., Dockter R.B.,
RA Fauchery L., Guy J., Iotti M., Le Tacon F., Lindquist E.A., Lipzen A.,
RA Malagnac F., Mello A., Molinier V., Miyauchi S., Poulain J., Riccioni C.,
RA Rubini A., Sitrit Y., Splivallo R., Traeger S., Wang M., Zifcakova L.,
RA Wipf D., Zambonelli A., Paolocci F., Nowrousian M., Ottonello S.,
RA Baldrian P., Spatafora J.W., Henrissat B., Nagy L.G., Aury J.M.,
RA Wincker P., Grigoriev I.V., Bonfante P., Martin F.M.;
RT "Pezizomycetes genomes reveal the molecular basis of ectomycorrhizal
RT truffle lifestyle.";
RL Nat. Ecol. Evol. 2:1956-1965(2018).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR000127-2};
CC -!- COFACTOR:
CC Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC Evidence={ECO:0000256|PIRSR:PIRSR000127-3};
CC Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC {ECO:0000256|PIRSR:PIRSR000127-3};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|PIRSR:PIRSR000127-3};
CC Note=Binds 2 [2Fe-2S] clusters. {ECO:0000256|PIRSR:PIRSR000127-3};
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DR EMBL; ML120527; RPA90391.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N4J1E1; -.
DR Proteomes; UP000276215; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 1.10.150.120; [2Fe-2S]-binding domain; 1.
DR Gene3D; 3.90.1170.50; Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead; 1.
DR Gene3D; 3.30.365.10; Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain; 4.
DR Gene3D; 3.30.390.50; CO dehydrogenase flavoprotein, C-terminal domain; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
DR InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
DR InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
DR InterPro; IPR016208; Ald_Oxase/xanthine_DH-like.
DR InterPro; IPR008274; AldOxase/xan_DH_MoCoBD1.
DR InterPro; IPR046867; AldOxase/xan_DH_MoCoBD2.
DR InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
DR InterPro; IPR005107; CO_DH_flav_C.
DR InterPro; IPR036683; CO_DH_flav_C_dom_sf.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR002346; Mopterin_DH_FAD-bd.
DR InterPro; IPR022407; OxRdtase_Mopterin_BS.
DR PANTHER; PTHR11908; XANTHINE DEHYDROGENASE; 1.
DR PANTHER; PTHR11908:SF100; XANTHINE DEHYDROGENASE; 1.
DR Pfam; PF01315; Ald_Xan_dh_C; 1.
DR Pfam; PF03450; CO_deh_flav_C; 1.
DR Pfam; PF00941; FAD_binding_5; 1.
DR Pfam; PF02738; MoCoBD_1; 1.
DR Pfam; PF20256; MoCoBD_2; 2.
DR PIRSF; PIRSF000127; Xanthine_DH; 2.
DR SMART; SM01008; Ald_Xan_dh_C; 1.
DR SMART; SM01092; CO_deh_flav_C; 1.
DR SUPFAM; SSF55447; CO dehydrogenase flavoprotein C-terminal domain-like; 1.
DR SUPFAM; SSF47741; CO dehydrogenase ISP C-domain like; 1.
DR SUPFAM; SSF54665; CO dehydrogenase molybdoprotein N-domain-like; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF56003; Molybdenum cofactor-binding domain; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
DR PROSITE; PS00559; MOLYBDOPTERIN_EUK; 1.
PE 4: Predicted;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714, ECO:0000256|PIRSR:PIRSR000127-3};
KW FAD {ECO:0000256|PIRSR:PIRSR000127-2};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000127-2};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000127-3};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR000127-
KW 3};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000127-3};
KW Molybdenum {ECO:0000256|ARBA:ARBA00022505, ECO:0000256|PIRSR:PIRSR000127-
KW 3}; Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000276215}.
FT DOMAIN 135..305
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT REGION 50..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1093
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-1"
FT BINDING 7
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT BINDING 9
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT BINDING 163..170
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 228
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 251
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 315
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 646
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT BINDING 677
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT BINDING 681
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 791
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT BINDING 793
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 941
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
SQ SEQUENCE 1157 AA; 126625 MW; 196283ADD8EE7E82 CRC64;
MLDGNLCRCM GYKPILDAAK SLVREDLGGV VFEGRSQNCG HPSRCCNDTP AAAAKPSRDE
SSSDETESPG ETSITETKEV PLSGATYGPP LKTCRCDDCC QLPPGGNKAT TEVDVLRGKY
PFPQFNFKSY ERHTEIIYLP VWFRPTTIEQ LVELPHTYPS AKIVAGSSEV QVEVHAREVW
SVGFKGFSIG EEKGEVVIGG NTSLTTPEKA CLEGCKKLGK RGKQLRYFAG RQIRNTAMPA
GNIVTASPIS DLNPVLIASG TVLTAQSKTR GEFPLLMKEF FVAYRTTALP ADSIITKLTI
PLPAEGTREV IKSYKQAKRK DDDIAIVTAG FRVVLDESSV VTDISLAYGG MAPKTVEAKN
SMEALLGKKL FDNTVLEDAV AAMEKDSPLG FTVPGGMPTY RKTLAFSFLF RFWHEVAAEL
ELGTQEQQVD HEIIEEIHRG ISYGSRDNDN PYEQRVVGKQ IPHLSGLKQA TGEAEYIDDM
PNIEGQLFGG LVLSKKAHAK LVKVDFTPAL QVPGVAGFVD INDLDDERNL WGSVKKDEPF
FAQDFVHSHG QPIGMVYAES AAIAQAAAQL VDVQYEELPP ILTISEAIAV KSFFPHGKMI
IRGKPTAEGF KDCDFVYEGH FYLETNAAAM IPRPEDREME VWSSTQNIME TQEFVSQVTG
VPSSRIVAKV KRMGGGFGGK ESRSMQLACI LAVGAKKVGR PIRCMLNRDE DMMTSGQRNP
FQAHCNVGVS KDGMLQVLDA DVYDNAGYSQ DLSGVVMDHA LTYMDSCYWI PHVHLRGHVC
KMNTHSNTTF RGFGAPQGQY IAECIITAIA DHLEMSVDEL QWKNLYKEGL LTPFLQHLED
WHVPQIITQL KAESDYDARI QQLEEFGLSF STAVHLNQAG ALVHIYDDGS ILLAHGGTEM
GQGLYAKTCQ IAAPEPNCPL DAIFTSKTSS NTVANTSPTA ASSGSDLNGM ARMNLSANGY
YKMPTIGYIW GNYVDPLPMC FYFTQGAAIS EVELDVLSGS HTGVRTDIKM DAGHSINPAI
NYGQIEGAFV QGQGLFTMEE TLWQKNCELF TRGPGTYKIP GFADIPQVFN VGLLKGMKWA
KLRSIQSSKG IGELPLFLGA SVLFALREAV KAARESVALD SPATAERMRV VVGDWIVRWA
KVEVKEGEKG FLVEAIA
//
