ID A0A3B5QN22_XIPMA Unreviewed; 570 AA.
AC A0A3B5QN22;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=sulfite oxidase {ECO:0000256|ARBA:ARBA00012505};
DE EC=1.8.3.1 {ECO:0000256|ARBA:ARBA00012505};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000032091.1, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000032091.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000032091.1};
RG Ensembl;
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_014326196.1; XM_014470710.1.
DR AlphaFoldDB; A0A3B5QN22; -.
DR STRING; 8083.ENSXMAP00000032091; -.
DR Ensembl; ENSXMAT00000036896.1; ENSXMAP00000032091.1; ENSXMAG00000023558.1.
DR GeneID; 102222788; -.
DR KEGG; xma:102222788; -.
DR CTD; 6821; -.
DR GeneTree; ENSGT00390000003749; -.
DR InParanoid; A0A3B5QN22; -.
DR OMA; VAQWARH; -.
DR OrthoDB; 1239at2759; -.
DR UniPathway; UPA00096; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
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:UP000002852}.
FT DOMAIN 94..172
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
SQ SEQUENCE 570 AA; 62919 MW; AD427E901E220572 CRC64;
MLLLRHCQSL TRLGAVGTLR YQATPCFASR AVRLCSSSRE DQKSYQRANW SANWKRIVAG
VLTGTGAVLT YGLLYQEVEQ ADAGLPTTEK RSSLPVFSHD EISKHRSLED GVWVTYKGGV
YDITEFVPMH PGGNKILLAA GGALEPFWAL YAVHDQEYVL EILSQYKVGE LSVEDLKKQH
NAKASDPYSS DPERHPVLRV NSKKPFNAEP PPEILTENYI TPHVLFFKRN HLPVPRVDPV
SYRLQVEGLP KGALTLSLKD LKTRFPKHTV TATLQCAGNR RSDMNKVKQV KGLNWGISAI
GNAKWSGARL RDVLLAAGFG PEVAKWARHV HFEGLDKDVT GSAYGTSIPI NKAMNEDGDV
LLAYEMNGED IPADHGFPVR VVVPGVVGAR NVKWLGRIVV STEESSSHWQ QLDYKGFSPG
TDWSKVDHAS SPAIQELPVQ SAITVPADGA EIDRSDETLT VKGYAWSGGG REVVRVDVSL
DGGKTWQVAQ LRSGDKGQPD EPSPPPGRAW AWKLWELTAP LPPDADELEI ICKAVDNSYN
VQPDSIPPIW NLRGLLSNAW HRVRVKVTED
//
