SUOX_MACFA
ID SUOX_MACFA Reviewed; 545 AA.
AC Q60HD0;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 3.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Sulfite oxidase, mitochondrial;
DE EC=1.8.3.1 {ECO:0000250|UniProtKB:Q07116};
DE Flags: Precursor;
GN Name=SUOX; ORFNames=QccE-18442 {ECO:0000303|Ref.1};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RA Kusuda J., Osada N., Tanuma R., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation and characterization of cDNA for macaque neurological disease
RT genes.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the oxidation of sulfite to sulfate, the terminal
CC reaction in the oxidative degradation of sulfur-containing amino acids.
CC {ECO:0000250|UniProtKB:Q07116}.
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:0000250|UniProtKB:Q07116};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24601;
CC Evidence={ECO:0000250|UniProtKB:Q07116};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000250|UniProtKB:Q07116};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group non-covalently
CC per subunit. {ECO:0000250|UniProtKB:Q07116};
CC -!- COFACTOR:
CC Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC Evidence={ECO:0000250|UniProtKB:Q07116};
CC Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC {ECO:0000250|UniProtKB:Q07116};
CC -!- PATHWAY: Energy metabolism; sulfur metabolism.
CC {ECO:0000250|UniProtKB:Q07116}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q07116}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC {ECO:0000250|UniProtKB:Q07116}.
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DR EMBL; AB125197; BAD51985.1; -; mRNA.
DR RefSeq; NP_001306533.1; NM_001319604.1.
DR AlphaFoldDB; Q60HD0; -.
DR SMR; Q60HD0; -.
DR STRING; 9541.XP_005571219.1; -.
DR PRIDE; Q60HD0; -.
DR GeneID; 102143378; -.
DR CTD; 6821; -.
DR eggNOG; KOG0535; Eukaryota.
DR eggNOG; KOG4576; Eukaryota.
DR UniPathway; UPA00096; -.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0043546; F:molybdopterin cofactor 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 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; 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; PS50255; CYTOCHROME_B5_2; 1.
DR PROSITE; PS00559; MOLYBDOPTERIN_EUK; 1.
PE 2: Evidence at transcript level;
KW Heme; Iron; Metal-binding; Mitochondrion; Molybdenum; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Transit peptide.
FT TRANSIT 1..79
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:Q07116"
FT CHAIN 80..545
FT /note="Sulfite oxidase, mitochondrial"
FT /id="PRO_0000006482"
FT DOMAIN 82..161
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT REGION 165..174
FT /note="Hinge"
FT /evidence="ECO:0000250|UniProtKB:P07850"
FT REGION 175..401
FT /note="Moco domain"
FT /evidence="ECO:0000250|UniProtKB:P07850"
FT REGION 402..538
FT /note="Homodimerization"
FT /evidence="ECO:0000250|UniProtKB:P07850"
FT BINDING 118
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 143
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 145
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000250|UniProtKB:P51687"
FT BINDING 147
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000250|UniProtKB:P07850"
FT BINDING 215..219
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:P07850"
FT BINDING 264
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 322
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:P07850"
FT BINDING 361
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:P07850"
FT BINDING 366
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:P07850"
FT BINDING 377..379
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:P07850"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51687"
SQ SEQUENCE 545 AA; 60193 MW; 72723BDBF7C14E77 CRC64;
MLLLHRAVVL RLQQACRLKS IPSRIYIQAC STNDSFRPQY PSLTFSGDNS STRGWKVMGT
LLGLGAVLAY QDHRCRAAQE STRIYTKEEV SSHTSPETGI WVALGSEVFD VTEFADLHPG
GPSKLMLAAG GPLEPFWALY AVHNQSHVRE LLAQYKVGEL NPEDKVAPTV ETSDPYADDP
VRHPALKVNS QRPFNAEPPP ELLTENYITP NPIFFTRNHL PVPNLDPDTY RLHIVGAPGG
QSLSLSLDDL HNFPKYEITV TLQCAGNRRS EMTQVKEVKG LEWRTGAIST ARWAGARLCD
VLAKAGHQLC ETEAHVCFEG LDSDPTGTAY GASIPLARAM DPEAGVLLAY EMNGQPLPRD
HGFPVRVVVP GVVGARHVKW LGRVSVQPEE SYSHWQRRDY KGFSPSVDWD TVDFDSAPSI
QELPVQSAIT EPRDGETVES GEVTIKGYAW SGGGRAVIRV DVSLDGGLTW QVAKLDGEEQ
RPRKAWAWRL WQLQAPVPAG QKELNIVCKA VDDGYNVQPD TVAPIWNLRG VLSNAWHRVH
VFVAP
