ID A0A0E0EA68_9ORYZ Unreviewed; 1344 AA.
AC A0A0E0EA68;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
OS Oryza meridionalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40149 {ECO:0000313|EnsemblPlants:OMERI07G08790.2};
RN [1] {ECO:0000313|EnsemblPlants:OMERI07G08790.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=OR44 {ECO:0000313|EnsemblPlants:OMERI07G08790.2};
RA Wing R.A., Panaud O., Henry R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OMERI07G08790.2}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={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|PIRSR:PIRSR000127-3};
CC Note=Binds 2 [2Fe-2S] clusters. {ECO:0000256|PIRSR:PIRSR000127-3};
CC -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00006849}.
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DR EnsemblPlants; OMERI07G08790.2; OMERI07G08790.2; OMERI07G08790.
DR Gramene; OMERI07G08790.2; OMERI07G08790.2; OMERI07G08790.
DR Proteomes; UP000008021; Chromosome 7.
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; 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 InterPro; IPR002888; 2Fe-2S-bd.
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; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR002346; Mopterin_DH_FAD-bd.
DR PANTHER; PTHR11908:SF89; ALDEHYDE OXIDASE-LIKE PROTEIN-RELATED; 1.
DR PANTHER; PTHR11908; 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; PF01799; Fer2_2; 1.
DR Pfam; PF02738; MoCoBD_1; 1.
DR Pfam; PF20256; MoCoBD_2; 2.
DR PIRSF; PIRSF000127; Xanthine_DH; 3.
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.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|PIRSR:PIRSR000127-3};
KW FAD {ECO:0000256|PIRSR:PIRSR000127-2};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000127-2};
KW Iron {ECO:0000256|PIRSR:PIRSR000127-3};
KW Iron-sulfur {ECO:0000256|PIRSR:PIRSR000127-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000127-3};
KW Molybdenum {ECO:0000256|PIRSR:PIRSR000127-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000008021}.
FT DOMAIN 255..442
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT ACT_SITE 1271
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-1"
FT BINDING 180
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT BINDING 183
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT BINDING 376..380
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 392
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 432
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 456
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 809
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 840
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 953
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 1127
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 1344 AA; 146699 MW; 0AEE0ECAC898CBE3 CRC64;
MHAIFTTTRR LAESYGGRRW EGEETLGYVL GRRWKARGCA ERLGVAEGWL GVNDRMRRRR
CPGSFPERDE VRAPELRIVG GWGDVRKGLR WSCHYGHLRW GGGAGGGRWF PKEEGTDVAW
AQVARRDFGM ALRWQVRSAL ARRGGGIHFC SIITTEGLGN TKDGFHAIQK RMSGFHASQC
GFCTPGMCMS IFSSLVNADK SKKPAPPKGF SKLSVSEAER SYHLPSYTLG GGICTFPDFL
KSEIKSSLDF NDASISGPRE GWYCPKSIKQ YYKLVNSGLF SESSVKVVVG NTSTGVYKDQ
DLYDKYIDIA GIPELSAIVR KDKGIEIGAA TSISKTIEIL NQESESTSSP NGSVVFRKLA
EHMSKVASPF VRNTASIGGN IILAHKYPFR SDIATILLGA AATVNLQVSS KTLHVNLEQF
LEQPPLDHST LLLSIFIPHW TSDCKKEHTL VFETYRAAPR PLGNAVSYVN SAFLGHVSLD
KSSGDNILSN LHLAFGAYGT EHAIRARKVE EYLTGKILSA SVVLEAIRLV RETIVPVEGT
THPEYRVSVA VGFLFSFLSP LCKGVIDPGK TLSISEDLVD TDNVHNMPLS SRRETLSGDE
YTPVGDPIKK YKVELQASGE AIYVDDIPAP KNCLYGEFIY STQPLANVKS IKFKPSLASK
KIITVVSAKD IPTGGRNIGS TFWFGDEEPL FGDPIAEFAG QALGVVIAET QRYADMAAKQ
AVVEYTTDGL KAPILTVEQA VQNNSYFQVP PERAPKQVGD FSKGMAEADH KIMSEEVKLA
SQYYFYMETQ TALAIPDEDN TMTVYSSSQF PELAQNVISK CLGIPFNNVR VITRRAGGGF
GGKAVRSLHI ATAAALCAHT LRRPVRMYLN RNTDMIMVGG RHPMKARYSV GFKSDGKITA
LHLDLLINAG ISADASPIIP GTIISGLKKY NWGALSFDVK LCKTNNTSKS VMRAPGETQG
SLIAEAIIEH VAAVLSLDAN TVRQRNFHSY DSLVLFYPES AGESSTYTLH SIFDRLASTS
SYLKRAESIK KFNSCNKWRK RGISSVPLIL KVRVRPAPGR VSVLSDGSIV IEVGGIELGQ
GLWTKVQQMA VYALGQLWPN GCEGLLDRIR VLQSDTLNLI QGGVTAGSTT SESSCAATLQ
ACNMLVERLK PVLDRLQLQS GIVSWDTLIS QVEIDLLTGA ITILRSDLIY DSGKSLNPAV
DLGQIEGSFI QGIGFFIYEE HQINSDGLVI SNSTWDYKIP SVDTIPKQFN VEVLNTGYHK
NRVLSSKASG EPAVVLGASV HCAVREAIQA ARIEFAGGSE STSSLLTFQL DVPAPMTLVK
ELCGLDIVEM YLEDLSSHGV GNCN
//
