ID O17505_BOMMO Unreviewed; 1120 AA.
AC O17505;
DT 01-JAN-1998, integrated into UniProtKB/TrEMBL.
DT 01-JAN-1998, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE SubName: Full=Xanthine dehydrogenase {ECO:0000313|EMBL:BAA21639.1};
DE Flags: Fragment;
GN Name=BmXDH2 {ECO:0000313|EMBL:BAA21639.1};
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091 {ECO:0000313|EMBL:BAA21639.1};
RN [1] {ECO:0000313|EMBL:BAA21639.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C108 {ECO:0000313|EMBL:BAA21639.1};
RC TISSUE=Posterior silk gland {ECO:0000313|EMBL:BAA21639.1};
RX PubMed=9927176; DOI=10.1046/j.1365-2583.1999.810073.x;
RA Komoto N., Yukuhiro K., Tamura T.;
RT "Structure and expression of tandemly duplicated xanthine dehydrogenase
RT genes of the silkworm (Bombyx mori).";
RL Insect Mol. Biol. 8:73-83(1999).
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 -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
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DR EMBL; AB005911; BAA21639.1; -; Genomic_DNA.
DR AlphaFoldDB; O17505; -.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
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; 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; 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; 1.
DR PIRSF; PIRSF000127; Xanthine_DH; 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 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 Peroxisome {ECO:0000256|ARBA:ARBA00023140}.
FT DOMAIN 25..210
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT REGION 325..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1052
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-1"
FT BINDING 53..60
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 132
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 142..146
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 155
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 218
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 558
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 589
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 593
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 671
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 703
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 705
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 870
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 NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAA21639.1"
SQ SEQUENCE 1120 AA; 123970 MW; EB1828B6A17FFFAF CRC64;
DPTQEPIFPP ELKLENEYST SYLVFRGENV IWLRPRNLKE LVLVKSRIPD SKVVVGNTEI
GVEMKFKKKF YPVLISPTII GEVNYCSIEN DGILVGAAVT LTELQIFLKS FIVEHPSKSK
IFKAVNAMLH WFAGSQVRNV ASLTGNIVTA SPISDLNPIL MACSAVLNVY STTNGSRQIT
IDENFFKGYR KTILEDDEVV ISIKLPFSTN DQYFKSYKQA RRRDDDISIV TAAFNVQFEG
NKVIKSKLCY GGMGPTTLLA SKSSKMLLGK HWNHETLSTV FHSLCEEFNL EFSVPGGMAE
YRKSLCLSLF FKFYLNVKDK LDISNGESST RPPKLSCGDE TRGEPSSSQY FEIRNSGEVD
ALGKPLPHAS AMKHATGEAI YCDDLPRIDG ELFLTLVLSS ESHAKIKSID TTAALSIPGV
VAFFCAKDLE VDRNIWGSII KDEEIFCSTY VTSRSCIVGA IVATSEIVAK KARDLVSITY
ERLQPVIVTL EDAIEHNSYF ENYPQTLSQG NVDEVFSKTK FTVEGKQRSG AQEHFYLETI
SAYAIRKEDE LEIICSSQSP SEIASFVSHT LGIPQHKVIA KVKRIGGGFG GKETRSSSLA
LPVAIAAYIL KKPVRSVLDR DEDIQMSGYR HPFLTKYKVA FDENGKISGA VFDVFANGGF
SMDLSCALIE RSTFHVDNCY SIPNIKINAY VCKTNLPSNT AFRGFGAPQV MLAAESMIRQ
IASTLGKSYE EIVEVNIYKE GSVTYYNQLL TYCTLSRCWN QCIDSSRYIA RKKAVNDFNR
SNRWKKKGIA LVPTKYGISF QTDVLMQAGA LLLVYNDGAV LLSIGGIEMG QGLFTKMIQI
ASKALEIEQS RIHISEAATD KIPNSTATAA SMSSDLYGMA VLNACNTLNQ RLKPYKTKDP
NGKWEDWVSE AYVDRVCLFA TGFYSAPKIE YNRNTNSGRL FEYFTYGVAC SEVIIDCLTG
DHEVLRTDIV MDVGESINPA IDIGQIEGAF MQGYGFLTME EVVFSANGET LSRGPGTYKI
PTLSDIPKEF NVSLLKGAPN PRAVYSSKAI GEPPLFLAAS VFFAIKEAIM AARSDSGVPV
EFELDAPATC ERIRMSCEDD ITLQVKPTVK RIGVPWNVIA
//
