ID A0A2U3XBW0_LEPWE Unreviewed; 628 AA.
AC A0A2U3XBW0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2021, sequence version 2.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=sulfite oxidase {ECO:0000256|ARBA:ARBA00012505};
DE EC=1.8.3.1 {ECO:0000256|ARBA:ARBA00012505};
GN Name=SUOX {ECO:0000313|RefSeq:XP_006728828.2};
OS Leptonychotes weddellii (Weddell seal) (Otaria weddellii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Phocidae;
OC Leptonychotes.
OX NCBI_TaxID=9713 {ECO:0000313|Proteomes:UP000245341, ECO:0000313|RefSeq:XP_006728828.2};
RN [1] {ECO:0000313|RefSeq:XP_006728828.2}
RP IDENTIFICATION.
RC TISSUE=Liver {ECO:0000313|RefSeq:XP_006728828.2};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes the oxidation of sulfite to sulfate, the terminal
CC reaction in the oxidative degradation of sulfur-containing amino acids.
CC {ECO:0000256|ARBA:ARBA00033734}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O2 + sulfite = H2O2 + sulfate; Xref=Rhea:RHEA:24600,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16189,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17359; EC=1.8.3.1;
CC Evidence={ECO:0000256|ARBA:ARBA00033649};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24601;
CC Evidence={ECO:0000256|ARBA:ARBA00033649};
CC -!- COFACTOR:
CC Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC Evidence={ECO:0000256|ARBA:ARBA00001924};
CC -!- PATHWAY: Energy metabolism; sulfur metabolism.
CC {ECO:0000256|ARBA:ARBA00004971}.
CC -!- PATHWAY: Sulfur metabolism. {ECO:0000256|ARBA:ARBA00004678}.
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DR RefSeq; XP_006728828.2; XM_006728765.2.
DR AlphaFoldDB; A0A2U3XBW0; -.
DR STRING; 9713.A0A2U3XBW0; -.
DR KEGG; lww:102734224; -.
DR OrthoDB; 1239at2759; -.
DR UniPathway; UPA00096; -.
DR Proteomes; UP000245341; Unplaced.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0008482; F:sulfite oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006790; P:sulfur compound metabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd02111; eukary_SO_Moco; 1.
DR Gene3D; 2.60.40.650; -; 1.
DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR Gene3D; 3.90.420.10; Oxidoreductase, molybdopterin-binding domain; 1.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR018506; Cyt_B5_heme-BS.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR005066; MoCF_OxRdtse_dimer.
DR InterPro; IPR008335; Mopterin_OxRdtase_euk.
DR InterPro; IPR000572; OxRdtase_Mopterin-bd_dom.
DR InterPro; IPR036374; OxRdtase_Mopterin-bd_sf.
DR PANTHER; PTHR19372:SF7; SULFITE OXIDASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR19372; SULFITE REDUCTASE; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF03404; Mo-co_dimer; 1.
DR Pfam; PF00174; Oxidored_molyb; 1.
DR PRINTS; PR00363; CYTOCHROMEB5.
DR PRINTS; PR00407; EUMOPTERIN.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF56524; Oxidoreductase molybdopterin-binding domain; 1.
DR PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE 4: Predicted;
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000245341}.
FT DOMAIN 165..244
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT REGION 245..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 628 AA; 69402 MW; 36DC81F55A163CCE CRC64;
METKNSLSSE LPSWRPACLR LQEAGTAAGR RPAASQWLGD ELRGESGPSL WTNVTVLAPP
LCPPSSGAGR VNQPQSRRRT RFATMLRHRA VISRLRQACR LQSVPSRLCI RACSTNDSLQ
PQCPSLAFSG DNSSPRGWRV MGTLLGLGAV LAYHDHRCRA AEKSPHIYTR EEVRSHSSPE
TRIWVTLGCE VFDVTEFVDL HPGGASKLML AAGGPLEPFW ALYAVHDQPH VREILAQYKV
GELSPEDKAP STLQTSDPYA DDPIRHPALK VNSQRPFNAE PPPELLTENY ITPNPIFFTR
NHLPVPNLDP ETYRLHVVGP PGCQSLFLSL DDLYQFPKHE ITVTLQCAGN RRSEMTWFKE
VKGLAWNTGA ISTACWAGAR LCDVLAKAGH QLCETEAHVC FEGLDSDPTG TAYGASIPLA
RAMDPEAEVL LAYEMNGQPL PRDHGFPVRV VVPGVVGARH VKWVGKVSVE PEESYSHWQR
RDYKGFSPSV DWDTVDFDSA PSIQELPVQS AITEPKDGET VQSGEVTIKG YAWSGGGRAV
VRVDVSLDGG LTWQVAELDG EEQRPRKAWA WRLWHLQAPV PAGKKELNIV CKAVDDSYNV
QPDTVAPIWN LRGVLSNAWH RVHVRVTP
//
