ID A0A3N4J6N4_9PEZI Unreviewed; 936 AA.
AC A0A3N4J6N4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Molybdenum cofactor-binding domain-containing protein {ECO:0000313|EMBL:RPA92100.1};
GN ORFNames=L873DRAFT_1794490 {ECO:0000313|EMBL:RPA92100.1};
OS Choiromyces venosus 120613-1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Tuberaceae; Choiromyces.
OX NCBI_TaxID=1336337 {ECO:0000313|EMBL:RPA92100.1, ECO:0000313|Proteomes:UP000276215};
RN [1] {ECO:0000313|EMBL:RPA92100.1, ECO:0000313|Proteomes:UP000276215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=120613-1 {ECO:0000313|EMBL:RPA92100.1,
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 -!- COFACTOR:
CC Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC Evidence={ECO:0000256|ARBA:ARBA00001924};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
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DR EMBL; ML120481; RPA92100.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N4J6N4; -.
DR STRING; 1336337.A0A3N4J6N4; -.
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:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.90.1170.50; Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead; 2.
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; 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 PANTHER; PTHR11908; XANTHINE DEHYDROGENASE; 1.
DR PANTHER; PTHR11908:SF100; XANTHINE DEHYDROGENASE; 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; 1.
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; 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.
PE 4: Predicted;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000276215}.
FT DOMAIN 185..367
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT REGION 82..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 936 AA; 102284 MW; 5EBD543A758E1852 CRC64;
MRGIVMSLYA LLQNSYDPVM RRYMLSEEME ELEELRPEDL DGVVFEGKKS KVEGKLGGNY
ISGAKGSGTG SCGRPGGCCK DTPAGTAKSS ADESLSDGTE ISSETSITET EEVPLSGAMY
GALLKTCERD DYYQLSSGVN KATTEVDVLG GKDSFPQFNF KSYEPHTEII YPLGLRKYTK
QPIFYGNEKK AWFRPTTIGQ LAELKHAYPP AEAVAGSSEV QVEVKFKHEN YGVSVYVGDI
EGLKGFSIGE EKGEVVIGGN TSLTVLEMVC LGGHKTLGKR GFILEAIRKQ LRYFAGRQIR
NTATPAGSIV TASPVWDLNP VLIASGAVLT AQSKTRGKFP LPMDEGVLCR LSDDGITLTI
PLPVEGTREV IKSYKQAKRK DDDIAIVKAR FRVLDESSVM DISQAYGGLP NESRMAPKTV
EAKNTKEALL GKKLFDNTVL EGAVAAMEKD SLVGFTVPGG MPTYCKTLAF SFLFRFWDGV
AAELELGTQV QQVDHEVIEE IHRGISYGSR DNDNPYEQRV TGEAEYIVDM LSIEGQLFGG
LVLSKKAHAK LAKVDFTPAE SAAIAQAAAQ LVDVQYEELP PILTISEAIA AKSFFPHGKM
LIRGKPTVET FKDCDFIYES ISRMDGQEYF YLETNAAAVI PRPEDGAMEV WSSTQNIMET
QEFVSQVTGA PSSRIVAKAK WMGGGFGGKE SRSVQLAYIL AVATKKVGRP IRRMLNCDED
MMTSGQRNPF QAHWKVGVSK AGMLKVLDAD IYNNAGYSQD LSGAIMDCAL THMDPCYWIP
HVHLRGHVCK TNTHSNTAFR FPRSTRSLEN VGRPAPLEFT ITQLKAESGH DARVQQAEES
NRMHKWKKRG ISLIPTKFGL SFATAVHLNQ AGALVHISND GSVLLALGGT EMGQGLHTKM
CQIAAQEQNC PLDAIFTSET SYNTVANTSS KKTRIS
//
