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Database: UniProt
Entry: H9GA43_ANOCA
LinkDB: H9GA43_ANOCA
Original site: H9GA43_ANOCA 
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
//
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