SUOX_CHICK
ID SUOX_CHICK Reviewed; 459 AA.
AC P07850;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2003, sequence version 3.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Sulfite oxidase;
DE EC=1.8.3.1 {ECO:0000305|PubMed:2687265};
GN Name=SUOX;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, AND CATALYTIC ACTIVITY.
RC TISSUE=Liver;
RX PubMed=2687265; DOI=10.1016/s0021-9258(19)30020-1;
RA Neame P.J., Barber M.J.;
RT "Conserved domains in molybdenum hydroxylases. The amino acid sequence of
RT chicken hepatic sulfite oxidase.";
RL J. Biol. Chem. 264:20894-20901(1989).
RN [2]
RP PROTEIN SEQUENCE OF 1-97.
RC TISSUE=Liver;
RX PubMed=510290; DOI=10.1111/j.1432-1033.1979.tb04187.x;
RA Guiard B., Lederer F.;
RT "Amino acid sequence of the 'b5-like' heme-binding domain from chicken
RT sulfite oxidase.";
RL Eur. J. Biochem. 100:441-453(1979).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 16-96.
RC STRAIN=White leghorn; TISSUE=Liver;
RA Binder C.M., Irminger J.C., Jaussi R.;
RL Submitted (MAR-1990) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP SEQUENCE REVISION TO 152, X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX
RP WITH HEME AND MO-MOLYBDOPTERIN, AND COFACTOR.
RC TISSUE=Liver;
RX PubMed=9428520; DOI=10.1016/s0092-8674(00)80488-2;
RA Kisker C., Schindelin H., Pacheco A., Wehbi W.A., Garrett R.M.,
RA Rajagopalan K.V., Enemark J.H., Rees D.C.;
RT "Molecular basis of sulfite oxidase deficiency from the structure of
RT sulfite oxidase.";
RL Cell 91:973-983(1997).
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:2687265}.
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:2687265};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24601;
CC Evidence={ECO:0000305|PubMed:2687265};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000269|PubMed:9428520};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group non-covalently
CC per subunit. {ECO:0000269|PubMed:9428520};
CC -!- COFACTOR:
CC Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC Evidence={ECO:0000269|PubMed:9428520};
CC Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC {ECO:0000269|PubMed:9428520};
CC -!- PATHWAY: Energy metabolism; sulfur metabolism.
CC {ECO:0000305|PubMed:2687265}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9428520}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC {ECO:0000250|UniProtKB:Q07116}.
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DR EMBL; X52559; CAA36793.1; -; mRNA.
DR PIR; A34180; A34180.
DR PDB; 1SOX; X-ray; 1.90 A; A/B=1-459.
DR PDB; 2A99; X-ray; 2.20 A; A=95-459.
DR PDB; 2A9A; X-ray; 2.00 A; A/B=95-459.
DR PDB; 2A9B; X-ray; 2.50 A; A=95-459.
DR PDB; 2A9C; X-ray; 2.50 A; A/B=95-459.
DR PDB; 2A9D; X-ray; 1.70 A; A/B=95-459.
DR PDB; 3HBG; X-ray; 1.90 A; A=1-459.
DR PDB; 3HBP; X-ray; 2.40 A; A=1-459.
DR PDB; 3HBQ; X-ray; 2.80 A; A=1-459.
DR PDB; 3R18; X-ray; 2.40 A; A=1-459.
DR PDB; 3R19; X-ray; 2.10 A; A=1-459.
DR PDBsum; 1SOX; -.
DR PDBsum; 2A99; -.
DR PDBsum; 2A9A; -.
DR PDBsum; 2A9B; -.
DR PDBsum; 2A9C; -.
DR PDBsum; 2A9D; -.
DR PDBsum; 3HBG; -.
DR PDBsum; 3HBP; -.
DR PDBsum; 3HBQ; -.
DR PDBsum; 3R18; -.
DR PDBsum; 3R19; -.
DR AlphaFoldDB; P07850; -.
DR SMR; P07850; -.
DR PRIDE; P07850; -.
DR VEuPathDB; HostDB:geneid_107055404; -.
DR InParanoid; P07850; -.
DR PhylomeDB; P07850; -.
DR BRENDA; 1.8.2.1; 1306.
DR BRENDA; 1.8.3.1; 1306.
DR UniPathway; UPA00096; -.
DR EvolutionaryTrace; P07850; -.
DR Proteomes; UP000000539; Unplaced.
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 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 3D-structure; Direct protein sequencing; Heme; Iron; Metal-binding;
KW Mitochondrion; Molybdenum; Oxidoreductase; Reference proteome.
FT CHAIN 1..459
FT /note="Sulfite oxidase"
FT /id="PRO_0000166076"
FT DOMAIN 4..83
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT REGION 83..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..95
FT /note="Hinge"
FT /evidence="ECO:0000305|PubMed:9428520"
FT REGION 96..323
FT /note="Moco domain"
FT /evidence="ECO:0000305|PubMed:9428520"
FT REGION 324..459
FT /note="Homodimerization"
FT /evidence="ECO:0000269|PubMed:9428520"
FT BINDING 40
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:0000269|PubMed:9428520"
FT BINDING 65
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:0000269|PubMed:9428520"
FT BINDING 69
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000269|PubMed:9428520"
FT BINDING 136..140
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000269|PubMed:9428520"
FT BINDING 185
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000269|PubMed:9428520"
FT BINDING 244
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000269|PubMed:9428520"
FT BINDING 283
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000269|PubMed:9428520"
FT BINDING 288
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000269|PubMed:9428520"
FT BINDING 299..301
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000269|PubMed:9428520"
FT CONFLICT 152
FT /note="R -> RR (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 9..12
FT /evidence="ECO:0007829|PDB:1SOX"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:1SOX"
FT STRAND 21..26
FT /evidence="ECO:0007829|PDB:1SOX"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:1SOX"
FT TURN 34..39
FT /evidence="ECO:0007829|PDB:1SOX"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:1SOX"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:1SOX"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:1SOX"
FT HELIX 56..61
FT /evidence="ECO:0007829|PDB:1SOX"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:1SOX"
FT HELIX 68..75
FT /evidence="ECO:0007829|PDB:1SOX"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:1SOX"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:1SOX"
FT TURN 96..99
FT /evidence="ECO:0007829|PDB:2A9D"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:2A9D"
FT TURN 112..115
FT /evidence="ECO:0007829|PDB:2A9D"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:2A9D"
FT HELIX 121..124
FT /evidence="ECO:0007829|PDB:2A9D"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:2A9D"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:2A9D"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:2A9D"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:2A9D"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:3HBG"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:2A9D"
FT HELIX 167..173
FT /evidence="ECO:0007829|PDB:2A9D"
FT STRAND 177..184
FT /evidence="ECO:0007829|PDB:2A9D"
FT TURN 186..189
FT /evidence="ECO:0007829|PDB:2A9D"
FT HELIX 190..194
FT /evidence="ECO:0007829|PDB:2A9D"
FT STRAND 208..218
FT /evidence="ECO:0007829|PDB:2A9D"
FT HELIX 219..225
FT /evidence="ECO:0007829|PDB:2A9D"
FT STRAND 237..245
FT /evidence="ECO:0007829|PDB:2A9D"
FT STRAND 251..257
FT /evidence="ECO:0007829|PDB:2A9D"
FT HELIX 258..262
FT /evidence="ECO:0007829|PDB:2A9D"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:2A9D"
FT STRAND 269..274
FT /evidence="ECO:0007829|PDB:2A9D"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:2A9D"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:2A9D"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:2A9D"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:2A9D"
FT STRAND 301..311
FT /evidence="ECO:0007829|PDB:2A9D"
FT HELIX 316..319
FT /evidence="ECO:0007829|PDB:2A9D"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:2A9D"
FT TURN 331..333
FT /evidence="ECO:0007829|PDB:2A9D"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:2A9D"
FT STRAND 348..354
FT /evidence="ECO:0007829|PDB:2A9D"
FT STRAND 362..372
FT /evidence="ECO:0007829|PDB:2A9D"
FT STRAND 379..391
FT /evidence="ECO:0007829|PDB:2A9D"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:3HBG"
FT STRAND 411..419
FT /evidence="ECO:0007829|PDB:2A9D"
FT STRAND 424..433
FT /evidence="ECO:0007829|PDB:2A9D"
FT HELIX 444..446
FT /evidence="ECO:0007829|PDB:2A9D"
SQ SEQUENCE 459 AA; 50205 MW; 7AA222AD7E4E77F1 CRC64;
APSYPRYTRE EVGRHRSPEE RVWVTHGTDV FDVTDFVELH PGGPDKILLA AGGALEPFWA
LYAVHGEPHV LELLQQYKVG ELSPDEAPAA PDAQDPFAGD PPRHPGLRVN SQKPFNAEPP
AELLAERFLT PNELFFTRNH LPVPAVEPSS YRLRVDGPGG RTLSLSLAEL RSRFPKHEVT
ATLQCAGNRR SEMSRVRPVK GLPWDIGAIS TARWGGASLR DVLLHAGFPE ELQGGEHVCF
EGLDADPGGA PYGASIPYGR ALSPAADVLL AYEMNGTELP RDHRFPVRVV VPGVVGARSV
KWLRRVAVSP DESPSRWQQN DYKGFSPCVD WDTVDYRTAP AIQELPVQSA VTQPRPGAAV
PPGELTVKGY AWSGGGREVV RVDVSLDGGR TWKVARLMGD KAPPGRAWAW ALWELTVPVE
AGTELEIVCK AVDSSYNVQP DSVAPIWNLR GVLSTAWHR
