ID A0A0D9VSA3_9ORYZ Unreviewed; 1231 AA.
AC A0A0D9VSA3;
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 Leersia perrieri.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR03G10410.1, ECO:0000313|Proteomes:UP000032180};
RN [1] {ECO:0000313|EnsemblPlants:LPERR03G10410.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:LPERR03G10410.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA Zhang J., Wing R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:LPERR03G10410.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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};
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DR AlphaFoldDB; A0A0D9VSA3; -.
DR STRING; 77586.A0A0D9VSA3; -.
DR EnsemblPlants; LPERR03G10410.1; LPERR03G10410.1; LPERR03G10410.
DR Gramene; LPERR03G10410.1; LPERR03G10410.1; LPERR03G10410.
DR eggNOG; KOG0430; Eukaryota.
DR Proteomes; UP000032180; Chromosome 3.
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; 3.10.20.30; -; 1.
DR Gene3D; 3.30.465.10; -; 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; 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; IPR012675; Beta-grasp_dom_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; 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; 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; 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 FAD {ECO:0000256|PIRSR:PIRSR000127-2};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000127-2};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000127-3};
KW Molybdenum {ECO:0000256|PIRSR:PIRSR000127-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000032180}.
FT DOMAIN 184..369
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT ACT_SITE 1167
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-1"
FT BINDING 212..219
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 292
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 302..306
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 359
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 377
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 723
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 742
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 746
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 824
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 856
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 858
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
SQ SEQUENCE 1231 AA; 135645 MW; 08F2FC6CBE50DA8C CRC64;
MASLTKAEEE TAAAEEWSDE AVIYVNSVRR VLRRPRAPHP APTSVFGEQS LDVVKVAVEP
ALHFAINACL APLYSVEGMH IITVEGIGNR QQDAFRVFSK RDDLLYIDSS PKNADGRPIC
PSTGKPCSCG DEKDTDASES SLLAHTKNYS PCSYNEIDGS VYSEKELIFP PELQLRKVMS
LKLNGFNGIK WYRPIKLKQV LHLKACYPNA KLINGNSEVG IETKFKNAQY SDLISVTHVP
ELHNLIMKED GIHIGSSVSL AQLQNFLRKV ILERDSHEIS SCEAVLRQLK WFAGTQIRNV
ASVGGNICTA SPISDLNPLW MATGATFEIL DVNNNIRTTP AKDFFLGYRK VDLKPDEILL
SVILPWTRPF EFVKEFKQAH RREDDIALVN AGMRVYIRKA KGDWIISDVS IVYGGVAAVP
LSASKTETFL TRKKWDYGLL DETFDLLKED ILLAENAPGG MVEFRNSLTL SFFFNFFLHV
NHEMNIKGFW KDGLPAASLS AIESYTRPVG VGIQCYELVR QGTAVGQPVV HMSSMLQVTG
EAEYTDDTPT PPNTLHAALV LSTKAHARIL CIDASLAKSS PGFVGLFLSK DVPGANHTGP
VVHDEEVFAS DVVTCVGQIV GIVVADTHDN AKAAANKVNI EYAELPAILS IEEAVKAGSF
HPNTKKCLVK GNVEECFVSG ACNRIIEGEV RVGGQEHFYM EPQCALVWPV DSGNEIHMIS
STQAPQKHQI VVCKTKRIGG GFGGKETRSA IFAAAASVAS YCLRRPVKIV LDRDVDMMTT
GQRHSFLGKY KVGFTNDGKI LALDLDLYNN GGNSLDLSLP VMERAMFHSD NVYDIPNIRV
SGQVCFTNFP SNTAFRGFGG PQAMLIAENW IQHMATELKR SPEEIKELNF QREGYVLHYG
QLLQNSTIRS VWDELKVSCN FIEARKAVIG FNNNNRWRKR GIAMVPTKFG ISFNSKFMNQ
AGALVQVYTD GTVLVAHGGV EMGQGIHTKV AQVAASSFNI PLSIGCMSTN HGSDLVQACY
MERIDLSAHG FYITPDVGFD WVSGKGTPFY YFTYGAAFAE VEIDTLTGDF HTRTVDIVMD
LGSSINPAID IGQIEGGFVQ GLGWVALEEL KWGDDNHKWI RPGHLFTCGP GSYKIPSVND
IPLNFKVSLL KGVSNPKVIH SSKAVGEPPF FLGSAVLFAI KDAIYAARAE EGHFDWFSLD
NPATPERIRM ACVDSITKKF ATIYYRPKLS V
//
