ID F1SPH2_PIG Unreviewed; 545 AA.
AC F1SPH2; A0A4X1W3T8;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 3.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=sulfite oxidase {ECO:0000256|ARBA:ARBA00012505};
DE EC=1.8.3.1 {ECO:0000256|ARBA:ARBA00012505};
GN Name=SUOX {ECO:0000313|Ensembl:ENSSSCP00000000396.4,
GN ECO:0000313|VGNC:VGNC:93621};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000000396.4, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000000396.4, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000000396.4,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:HDB44506.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=30723633; DOI=.7717/peerj.6374;
RA Gilbert D.G.;
RT "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL PeerJ 7:E6374-E6374(2019).
RN [3] {ECO:0000313|Ensembl:ENSSSCP00000000396.4}
RP IDENTIFICATION.
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 EMBL; DQIR01189029; HDB44506.1; -; Transcribed_RNA.
DR STRING; 9823.ENSSSCP00000000396; -.
DR PaxDb; 9823-ENSSSCP00000025055; -.
DR Ensembl; ENSSSCT00000000402.5; ENSSSCP00000000396.4; ENSSSCG00000000376.5.
DR Ensembl; ENSSSCT00005017976.1; ENSSSCP00005010757.1; ENSSSCG00005011651.1.
DR Ensembl; ENSSSCT00005018032.1; ENSSSCP00005010791.1; ENSSSCG00005011651.1.
DR VGNC; VGNC:93621; SUOX.
DR GeneTree; ENSGT00390000003749; -.
DR HOGENOM; CLU_003827_5_1_1; -.
DR TreeFam; TF300905; -.
DR Reactome; R-SSC-1614517; Sulfide oxidation to sulfate.
DR UniPathway; UPA00096; -.
DR Proteomes; UP000008227; Chromosome 5.
DR Bgee; ENSSSCG00000000376; Expressed in metanephros cortex and 42 other cell types or tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IBA:GO_Central.
DR GO; GO:0008482; F:sulfite oxidase activity; IBA:GO_Central.
DR GO; GO:0006790; P:sulfur compound metabolic process; IBA:GO_Central.
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 1: Evidence at protein level;
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 Proteomics identification {ECO:0007829|PeptideAtlas:F1SPH2};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227}.
FT DOMAIN 82..161
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT REGION 163..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 545 AA; 60410 MW; DCB56335CC89F923 CRC64;
MLLLRKVVLP GIQQACRLKS TPSRLCIQAC STNDSFQPQH HILAFSGDHS STKGWRVMGT
LLGLGAVLAY HDYQCKAAQE PPRIYTREEV RSHSSPETGI WVTLGSEVFD VTEFVDLHPG
GPSKLMLAAG GPLEPFWALY AVHDQPHVRE ILAQYKIGEL SPEDKAPSTL KTSDPYANDP
IRHPALKVNS QRPFNAEPPP ELLTENYITP NPIFFTRNHL PVPNLDPDTY RLHVVGPPGG
QSLYLSLDDL YQFPKHEITV TLQCAGNRRS EMTRFKEVRG LEWNTGAIST ARWAGARLCD
VLAQAGHQLS EAEAHVCFEG LDSDPTGTAY GASIPLARAM DPEAEVLLAY EMNGQPLPRD
HGFPVRVVVP GVVGARHVKW LGKVSVEPEE SHSHWQRRDY KGFSPSVDWD TVDFDSAPSI
QELPVQSAIT QPKDGETIES REVTIKGYAW SGGGRAVVRV DVSLDGGLTW QAAELDGEEQ
RPRKAWAWRL WQLQAPVPAG KKELNIICKA VDDSYNVQPD TVAPIWNLRG VLSNAWHRIH
VHVAP
//
