ID A0A1D6HX73_MAIZE Unreviewed; 1286 AA.
AC A0A1D6HX73;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Aldehyde oxidase/xanthine dehydrogenase molybdopterin binding protein {ECO:0000313|EMBL:ONM52811.1};
GN ORFNames=ZEAMMB73_Zm00001d019376 {ECO:0000313|EMBL:ONM52811.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:ONM52811.1};
RN [1] {ECO:0000313|EMBL:ONM52811.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Seedling {ECO:0000313|EMBL:ONM52811.1};
RG Maize Genome Sequencing Project;
RA Ware D.;
RT "Update maize B73 reference genome by single molecule sequencing
RT technologies.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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 EMBL; CM007650; ONM52811.1; -; Genomic_DNA.
DR EMBL; CM007650; ONM52812.1; -; Genomic_DNA.
DR ExpressionAtlas; A0A1D6HX73; baseline and differential.
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; 1.
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.
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}.
FT DOMAIN 130..318
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT ACT_SITE 1211
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-1"
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 12
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT BINDING 56
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT BINDING 58
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT BINDING 252..256
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 268
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 308
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 332
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 685
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 716
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 829
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 1006
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 1286 AA; 139082 MW; 9E179C8E48BC2439 CRC64;
MSGFHASQCG FCTPGMCMSI FTSLIKADKS KRPEPPKGFS KLKVSEAGKA FSGNLCRCTG
YRPIVDACKS FASDVDLEDL GLNIFWKKGD RNPDVSELPS YTLGGGVCTF PDFLKTELKS
SLDHLNNPCI AASGEGWYHP KSIKEYYELI NSCLFSDSVK VVVGNTSSGV PGYKDQDIYS
KYIDIGGIPE LSNIVRMGSG IEIGVATSIS RTIEILEEEC ESISSPNGSV VFRKLANHMS
KVATPFVRNT ASIGGNIVLA QKFPFPSDIA TILLGAGATV CLQVVAERRQ ITLEEFLEQP
PIDATTLLLS IFIPNWISDS GANISLLFET YRAAPRPLGN AVSYVNCAFL GHASLDEQSD
TLVLSNLRLA FGAYGTEHAI RATRVEEFLT GKSLTASVVL GAIQLLRETV VPMEGTSHPE
YRVSAAVGFL FSFLSPFSKC IPEPGKSLAS SSTDSADTDD VRNLPLSTRR ETFSSDEYKP
VGEPIKKYGV ELQASGEAVY VDDIPAPKNC LYGEFIYSTQ PLAYVKSIKF KSSLASEKII
SFVSAKDIPS GGLNIGSSST FGDEPLFGDP IAEYAGQALG IVIAETQRYA DMAAKQVVIE
YDTEDLSPPI ITVEQAVEKS SYFDVPPEFY PKEVGDVSKG MAEADHKIPS TEVKLASEYY
FYMETQTALA VPDEDNTLVV YSSSQYPELA QSVIARCLGI PFSNVRVITR RVGGGFGGKA
FRSFQVATAA ALCAYKLRRP VRMYLNRNTD MVMVGGRHPV KAHYTVGFKN DGNVTALHLD
LLINAGISPD ASPIIPGTII SSVKKYNWGA LSFDIKLCRT NNSSKSVMRA PGDTQGSLIA
DAVIEHVASV LSLDANSVRE KNFHTYGTLQ SFYPDSAGEA STYTLHSIFD RLVSTSSYLD
RAESIKEFNS NSKWRKRGIS CVPLIFKVEP RAAPGRVSVL KDGSVVVEVG GIEIGQGLWT
KVQQMTAFAL GRLWPDADGG GECLLGRVRV LQADTLNLVQ GGLTAGSTAS ESSCAATLQA
CNTLYDRLKL VLDRLQQRSE NVSWDTLVSQ ASLSSSLVRS HRLLFPAIRK MSCGVSMMQA
YEDDVDLSAS AYWVPGQASN KYLNYGAGIS EVEIDLLTGA ITIIRGDLVY DCGKSLNPAV
DLGQIEGSFV QGIGFFVYEE YTTNSDGLMI SNSTWDYKIP SVDIIPRQFN AEVLNTGYHK
NRVLSSKASG EPALVLASSV HCALREAIRA ARVEFADSTV SSGHSPLEFQ MGVPAPMTLV
KELCGLDIVD RYLEGLSTCE RAAGGA
//
