SUOX_RAT
ID SUOX_RAT Reviewed; 546 AA.
AC Q07116; Q6P6W0;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Sulfite oxidase, mitochondrial {ECO:0000303|PubMed:15489334};
DE EC=1.8.3.1 {ECO:0000305|PubMed:8276806};
DE Flags: Precursor;
GN Name=Suox {ECO:0000312|RGD:619994};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 43-546, FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, AND COFACTOR.
RC TISSUE=Liver;
RX PubMed=8276806; DOI=10.1016/s0021-9258(17)42345-3;
RA Garrett R.M., Rajagopalan K.V.;
RT "Molecular cloning of rat liver sulfite oxidase. Expression of a eukaryotic
RT Mo-pterin-containing enzyme in Escherichia coli.";
RL J. Biol. Chem. 269:272-276(1994).
RN [3]
RP PROTEIN SEQUENCE OF 98-253; 256-275; 280-433; 485-495 AND 503-537.
RC TISSUE=Liver;
RX PubMed=2249998; DOI=10.1016/s0021-9258(17)45303-8;
RA Barber M.J., Neame P.J.;
RT "A conserved cysteine in molybdenum oxotransferases.";
RL J. Biol. Chem. 265:20912-20915(1990).
RN [4]
RP PROTEIN SEQUENCE OF 187-201 AND 340-368.
RC TISSUE=Liver;
RX PubMed=3393528; DOI=10.1073/pnas.85.14.5006;
RA Crawford N.M., Smith M., Bellissimo D.B., Davis R.W.;
RT "Sequence and nitrate regulation of the Arabidopsis thaliana mRNA encoding
RT nitrate reductase, a metalloflavoprotein with three functional domains.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:5006-5010(1988).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=6181785; DOI=10.1016/0006-291x(82)91698-9;
RA Ono H., Ito A.;
RT "Evidence for participation of the inner membrane in the import of sulfite
RT oxidase into the intermembrane space of liver mitochondria.";
RL Biochem. Biophys. Res. Commun. 107:258-264(1982).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RA Maurya D.K., Bhargava P.;
RL Submitted (DEC-2008) 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:0000269|PubMed:8276806}.
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:0000305|PubMed:8276806};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24601;
CC Evidence={ECO:0000305|PubMed:8276806};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000269|PubMed:8276806};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group non-covalently
CC per subunit. {ECO:0000269|PubMed:8276806};
CC -!- COFACTOR:
CC Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC Evidence={ECO:0000269|PubMed:8276806};
CC Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC {ECO:0000269|PubMed:8276806};
CC -!- PATHWAY: Energy metabolism; sulfur metabolism.
CC {ECO:0000269|PubMed:8276806}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8276806}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC {ECO:0000269|PubMed:6181785, ECO:0000269|PubMed:8276806}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA16618.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC061991; AAH61991.2; -; mRNA.
DR EMBL; L05084; AAA16618.1; ALT_INIT; mRNA.
DR PIR; A53107; A53107.
DR RefSeq; NP_112389.3; NM_031127.3.
DR AlphaFoldDB; Q07116; -.
DR SMR; Q07116; -.
DR STRING; 10116.ENSRNOP00000008018; -.
DR CarbonylDB; Q07116; -.
DR iPTMnet; Q07116; -.
DR PhosphoSitePlus; Q07116; -.
DR jPOST; Q07116; -.
DR PaxDb; Q07116; -.
DR PRIDE; Q07116; -.
DR GeneID; 81805; -.
DR KEGG; rno:81805; -.
DR UCSC; RGD:619994; rat.
DR CTD; 6821; -.
DR RGD; 619994; Suox.
DR eggNOG; KOG0535; Eukaryota.
DR eggNOG; KOG4576; Eukaryota.
DR InParanoid; Q07116; -.
DR PhylomeDB; Q07116; -.
DR Reactome; R-RNO-1614517; Sulfide oxidation to sulfate.
DR UniPathway; UPA00096; -.
DR PRO; PR:Q07116; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IDA:RGD.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IDA:RGD.
DR GO; GO:0008482; F:sulfite oxidase activity; IDA:RGD.
DR GO; GO:0007584; P:response to nutrient; IDA:RGD.
DR GO; GO:0006790; P:sulfur compound metabolic process; IBA:GO_Central.
DR Gene3D; 3.10.120.10; -; 1.
DR Gene3D; 3.90.420.10; -; 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 InterPro; IPR022407; OxRdtase_Mopterin_BS.
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; SSF55856; 1.
DR SUPFAM; SSF56524; SSF56524; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR PROSITE; PS00559; MOLYBDOPTERIN_EUK; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Heme; Iron; Metal-binding; Mitochondrion;
KW Molybdenum; Oxidoreductase; Phosphoprotein; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..80
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:8276806"
FT CHAIN 81..546
FT /note="Sulfite oxidase, mitochondrial"
FT /id="PRO_0000006484"
FT DOMAIN 83..162
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT REGION 166..175
FT /note="Hinge"
FT /evidence="ECO:0000250|UniProtKB:P07850"
FT REGION 176..402
FT /note="Moco domain"
FT /evidence="ECO:0000250|UniProtKB:P07850"
FT REGION 403..539
FT /note="Homodimerization"
FT /evidence="ECO:0000250|UniProtKB:P07850"
FT BINDING 119
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT BINDING 144
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT BINDING 146
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000250|UniProtKB:P51687"
FT BINDING 148
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000250|UniProtKB:P07850"
FT BINDING 216..220
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:P07850"
FT BINDING 265
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000250|UniProtKB:P07850"
FT BINDING 323
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:P07850"
FT BINDING 362
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:P07850"
FT BINDING 367
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:P07850"
FT BINDING 378..380
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:P07850"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51687"
FT CONFLICT 98
FT /note="K -> Q (in Ref. 2; AAA16618)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="S -> T (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="W -> R (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="C -> Q (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="A -> G (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="H -> S (in Ref. 3; AA sequence and 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 394..396
FT /note="SHW -> HYL (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 432
FT /note="Q -> V (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 514
FT /note="D -> A (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 527
FT /note="W -> A (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 546 AA; 60806 MW; B4A4E46A8F15765D CRC64;
MLPRLYRSVA VGLPRAIRAK STPLRLCIQA CSSSDSLKPQ HPSLTFSDDN SRTRGWKVMG
TLIGLGAVLA YHDHRCRASQ ESPRIYSKED VRSHNNLKTG VWVTLGSEVF DVTKFVDLHP
GGQSKLMLAA GGPLEPFWAL YAVHNQPHVR ELLAEYKIGE LNPEDRMSPP LEASDPYSND
PMRHPALRIN SQRPFNAEPP PELLTESYIT PNPIFFTRNH LPVPNLDPDT YRLHVVGAPG
GQSLSLSLDD LHKFPKHEVT VTLQCAGNRR SEMNKVKEVK GLEWRTGAIS TARWAGARLC
DVLAQAGHRL RETEAHVCFE GLDSDPTGTA YGASIPLARA MDPQAEVLLA YEMNGQPLPR
DHGFPVRVVV PGVVGARHVK WLGRVSVESE ESYSHWQRRD YKGFSPSVDW DTVDFDLAPS
IQELPIQSAI TQPQDGTTVE SGEVIIKGYA WSGGGRAVIR VDVSMDGGLT WQEAELEGEE
QHPRKAWAWR IWQLKAHVPA EQKELNIICK AVDDSYNVQP DTVAPIWNLR GVLSNAWHRV
HVQVVP
