ID   A0A0N5APD5_9BILA        Unreviewed;       500 AA.
AC   A0A0N5APD5;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=sulfite oxidase {ECO:0000256|ARBA:ARBA00012505};
DE            EC=1.8.3.1 {ECO:0000256|ARBA:ARBA00012505};
OS   Syphacia muris.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Syphacia.
OX   NCBI_TaxID=451379 {ECO:0000313|Proteomes:UP000046393, ECO:0000313|WBParaSite:SMUV_0000650801-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SMUV_0000650801-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
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   -!- SIMILARITY: Belongs to the cytochrome b5 family.
CC       {ECO:0000256|RuleBase:RU362121}.
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DR   AlphaFoldDB; A0A0N5APD5; -.
DR   STRING; 451379.A0A0N5APD5; -.
DR   WBParaSite; SMUV_0000650801-mRNA-1; SMUV_0000650801-mRNA-1; SMUV_0000650801.
DR   UniPathway; UPA00096; -.
DR   Proteomes; UP000046393; Unplaced.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR   GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
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; 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; 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   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; PS00191; CYTOCHROME_B5_1; 1.
DR   PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR   PROSITE; PS00559; MOLYBDOPTERIN_EUK; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU362121};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU362121};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU362121}; Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          51..129
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
SQ   SEQUENCE   500 AA;  56799 MW;  90372B93D2DEA135 CRC64;
     LACSGVFYYK RQYLTAYAAT ATTLNQQQQQ PATEFPSSNT FKVNVLPRKD LPTYRLDEVK
     KHGKSAERIW VTFQQGVYDI TDFIEGHPGG NKILMAAGGS IEPYWHLYQQ HENEETYEML
     EELRIGNLDP RDVDKDDLYA NDPLRHPALQ VLSQKPFNAE TPSQLLIDHF YTPNPLFFVR
     SHMPVPKTHR VEIDGIGVKK PLSFNVDELK KQFEVVSVSA TLQCAGNRRA DMSKEKTVQG
     LPWKGSAISN AKWTGVRLRD VLVAAGVDPN DKRIKHVHFE GADHDTEGQH FGSSISFEKA
     MKSEVLLAFM MNDEEIPLDH GYPLRLVAPG IAGVRNVKWL KKIRLSDEES PAFWQQKDYK
     FTEKINYDAV PAIQEYPVQS AFVIPSENIT VKRGLTYLEV AGYAWSGGGR GIIRVEVSAD
     GGNTWQRAEL EQNPDEDLDH MWSWTFFRAT IQIPPNVKEM DLVCKATDRS YNTQPETARG
     TWNVRGLLNN AWHHIKVNVV
//