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Database: UniProt
Entry: A0A384AVM2_BALAS
LinkDB: A0A384AVM2_BALAS
Original site: A0A384AVM2_BALAS 
ID   A0A384AVM2_BALAS        Unreviewed;      1333 AA.
AC   A0A384AVM2;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   13-SEP-2023, entry version 19.
DE   RecName: Full=Xanthine dehydrogenase/oxidase {ECO:0000256|ARBA:ARBA00019137};
DE            EC=1.17.1.4 {ECO:0000256|ARBA:ARBA00013123};
DE            EC=1.17.3.2 {ECO:0000256|ARBA:ARBA00013221};
GN   Name=XDH {ECO:0000313|RefSeq:XP_007191440.1};
OS   Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS   (Balaenoptera davidsoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC   Balaenopteridae; Balaenoptera.
OX   NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007191440.1};
RN   [1] {ECO:0000313|RefSeq:XP_007191440.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_007191440.1};
RG   RefSeq;
RL   Submitted (JAN-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + NAD(+) + xanthine = H(+) + NADH + urate;
CC         Xref=Rhea:RHEA:16669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17712, ChEBI:CHEBI:17775, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.17.1.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00000532};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O2 + xanthine = H2O2 + urate; Xref=Rhea:RHEA:21132,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:17712, ChEBI:CHEBI:17775; EC=1.17.3.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00000029};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + hypoxanthine + NAD(+) = H(+) + NADH + xanthine;
CC         Xref=Rhea:RHEA:24670, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17368, ChEBI:CHEBI:17712, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.17.1.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00000239};
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   -!- 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   -!- SUBUNIT: Homodimer. Interacts with BTN1A1.
CC       {ECO:0000256|ARBA:ARBA00026017}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
CC   -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00006849}.
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DR   RefSeq; XP_007191440.1; XM_007191378.1.
DR   GeneID; 103004564; -.
DR   CTD; 7498; -.
DR   OrthoDB; 5485853at2759; -.
DR   Proteomes; UP000261681; Unplaced.
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:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0004854; F:xanthine dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004855; F:xanthine oxidase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.10.20.30; -; 1.
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; 5.
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; IPR002888; 2Fe-2S-bd.
DR   InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
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.
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   InterPro; IPR022407; OxRdtase_Mopterin_BS.
DR   InterPro; IPR014307; Xanthine_DH_ssu.
DR   NCBIfam; TIGR02963; xanthine_xdhA; 1.
DR   PANTHER; PTHR45444; XANTHINE DEHYDROGENASE; 1.
DR   PANTHER; PTHR45444:SF3; 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; PF00111; Fer2; 1.
DR   Pfam; PF01799; Fer2_2; 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; SSF54292; 2Fe-2S ferredoxin-like; 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; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
DR   PROSITE; PS00559; MOLYBDOPTERIN_EUK; 1.
PE   3: Inferred from homology;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714, ECO:0000256|PIRSR:PIRSR000127-3};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000127-2};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000127-3};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR000127-
KW   3};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000127-3};
KW   Molybdenum {ECO:0000256|ARBA:ARBA00022505, ECO:0000256|PIRSR:PIRSR000127-
KW   3}; Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261681}.
FT   DOMAIN          4..91
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          229..414
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   ACT_SITE        1262
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-1"
FT   BINDING         43
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT   BINDING         48
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT   BINDING         51
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT   BINDING         73
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT   BINDING         113
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT   BINDING         116
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT   BINDING         148
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT   BINDING         150
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT   BINDING         257..264
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT   BINDING         337
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT   BINDING         360
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT   BINDING         404
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT   BINDING         422
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT   BINDING         768
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         799
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         803
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT   BINDING         881
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT   BINDING         913
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         915
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT   BINDING         1011
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT   BINDING         1080
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   1333 AA;  146917 MW;  B7A20F19C072CF06 CRC64;
     MTADELVFFV NGKKVVEKNA DPETTLLAYL RRKLGLRGTK LGCGEGGCGA CTVMLSKYDR
     LQDKIIHFSA NACLAPICSL HHVAVTTVEG IGSTKTRLHP VQERIAKSHG SQCGFCTPGI
     VMSMYTLLRN QPEPTVEEIE DAFQGNLCRC TGYRPILQGF RTFAKDGGCC GGNGNNPNCC
     MNQKKDHKVT LSPSLFNPEE FMPLDPTQEP IFPPELLRLK DIPQKQLRFE GERVTWIQAS
     ALTELLDLKA QHPEAKLVVG NTEIGIEMKF KNQLFPVIIC PAWIPELNSV EHGLEGISFG
     AACSLNSVEK TLLDAVAKLP TQKTEVFRGV LQQLRWFAGK QVKSVACIGG NIITASPISD
     LNPVFMASGT KLTIVSRGTR RTVPMDHTFF PGYRKTLLGP EEILLSIEIP YSREGEFFSA
     FKQASRREDD IAKVTCGMRV LLQPGTTQVK ELALCYGGMA DRTISALKTT QKQLLKFWNE
     ELLQDVCAGL VEELPLSPDA PGGMIEFRRT LTLSFFFKFY LTVLQKLGKE DSEDKCGKLD
     PTYSSATLLF HKDPPANIQL FQEVPKGQSE EDMVGRPLPH LAAALQASGE AVYCDDIPRY
     ENELFLRLVI STRAHAKIKS IDISEAQKVP GFVCFLSADD IPGSNETGLF NDETVFAKDE
     VTCVGHVIGA VVADTPEHAQ RAAHGVKVTY EDLPAIITIE DAIKNNSFYG SELKIEKGDL
     KKGFSEADNV VSGELYIGGQ EHFYLETHCA IAVPKGEAGE MELFASTQNI MSTQSFVAKM
     LGVPINRILV RVKRMGGGFG GKETRGIMMT VAVALAAYKT GYPVRCMLDR DEDMLITGGR
     HPFLARYKVG FMKTGKIVAL EVDHYSNVGN SQDLSLGIME RALFHMDNSY KIPNVRGTGR
     LCKTNLPSNT AFRGFGGPQA LFIAEHWMSD VAVTCGLPAE EVRRKNLYRE GDLTHFNQRL
     EGFNLPRCWD ECLKSSQYHD RKTEVDKFNK ENCWKKRGLC IIPTKFGISF TVPFLNQAGA
     LIHVYTDGSV LVSHGGTEMG QGLHTKMVQV ASRALKIPTS KIYISETSTN TVPNSSPTAA
     SVSTDIYGQA VYEACQTILK RLEPFKRKDP SGSWEDWVMA AYRGTVSLSA TGFYRTPNLG
     YSFATNSGNA FHYFTYGVAC SEVEIDCLTG DHKNLRTDIV MDVGSSLNPA IDIGQVEGAF
     VQGLGLFTLE ELHYSPEGSL HTRGPSTYKI PAFGSIPTEF RVSLLRDCPN RKAIYASKAV
     GEPPLFLGAS IFFAIKDAIR AARAQHTDNN TKELFRLDSP ATPEKIRNAC VDKFTTLCVT
     DVPENCKPWS LKV
//
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