ID H9GA43_ANOCA Unreviewed; 555 AA.
AC H9GA43;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 24-JAN-2024, entry version 55.
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:ENSACAP00000005234.3};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000005234.3, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000005234.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000005234.3};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000005234.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-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}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC {ECO:0000256|ARBA:ARBA00004569}.
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DR RefSeq; XP_008112632.1; XM_008114425.2.
DR RefSeq; XP_008112633.1; XM_008114426.2.
DR AlphaFoldDB; H9GA43; -.
DR STRING; 28377.ENSACAP00000005234; -.
DR Ensembl; ENSACAT00000005351.3; ENSACAP00000005234.3; ENSACAG00000005368.3.
DR GeneID; 100555738; -.
DR KEGG; acs:100555738; -.
DR CTD; 6821; -.
DR eggNOG; KOG0535; Eukaryota.
DR eggNOG; KOG4576; Eukaryota.
DR GeneTree; ENSGT00390000003749; -.
DR HOGENOM; CLU_003827_5_1_1; -.
DR InParanoid; H9GA43; -.
DR TreeFam; TF300905; -.
DR UniPathway; UPA00096; -.
DR Proteomes; UP000001646; Unplaced.
DR Bgee; ENSACAG00000005368; Expressed in heart and 12 other cell types or tissues.
DR GO; GO:0016020; C:membrane; 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; 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 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; PS50255; CYTOCHROME_B5_2; 1.
DR PROSITE; PS00559; MOLYBDOPTERIN_EUK; 1.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004}; Membrane {ECO:0000256|SAM:Phobius};
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:UP000001646};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 95..174
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT REGION 172..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..190
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 555 AA; 61437 MW; 65F1B6EC24C9D616 CRC64;
MLLSRPTWSG LSTLQRTCWL RAMVQRTFPV APLAWTRFHS HNTWNEAGGP RRRRLVGVAV
VAGAGLGIGT ILAYGDLHQK AAKAETPESA SDPQFPTFTR QEVARHHSEA SRVWVTYGSD
VFDITDFIEQ HPGGKSKILL AAGGALEPFW ALYAMHNQEH VLEILQGFKV GQLSPEEPPQ
PTPGDPYADD PPRHPALQTN TLKPFNAEPP PELISENYLT PNQLFFKRNH LPVPNVDPAT
YRLHVGGPRG RTLSLSLQDL KKFPKHEVTA ALQCAGNRRA EMNSLKNTNR LGWNIGAISN
ARWGGARLRD VLMQAGYKQD DEGHVCFEGL DKDQSGTVYG ASIPFKKAMC LEGDVLLAYE
MNGEELPRDH GFPLRVLVPG IVGARNVKWL ARITVSPEES PSHWQQKDYK GFSPGVTWDT
VDFSKAPAIQ DMPVQSAITE PSPQTTISPG ELTVKGYAWS GGGRRIIRVD VSLDGGKSWR
EAELTGERQL PGRAWAWQLW QLNVSVPAGT RELNVVCKAV DTSYNEQPDT VGPIWNILGV
LNNAWHRVHL LVAED
//