ID A0A0V1MDT3_9BILA Unreviewed; 662 AA.
AC A0A0V1MDT3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=sulfite oxidase {ECO:0000256|ARBA:ARBA00012505};
DE EC=1.8.3.1 {ECO:0000256|ARBA:ARBA00012505};
GN ORFNames=T10_1595 {ECO:0000313|EMBL:KRZ69763.1};
OS Trichinella papuae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ69763.1, ECO:0000313|Proteomes:UP000054843};
RN [1] {ECO:0000313|EMBL:KRZ69763.1, ECO:0000313|Proteomes:UP000054843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ69763.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRZ69763.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JYDO01000129; KRZ69763.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1MDT3; -.
DR STRING; 268474.A0A0V1MDT3; -.
DR UniPathway; UPA00096; -.
DR Proteomes; UP000054843; Unassembled WGS sequence.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
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; 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 4: Predicted;
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
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:UP000054843}.
FT DOMAIN 81..159
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
SQ SEQUENCE 662 AA; 74077 MW; 38B3A2E1FE54CD10 CRC64;
MRIIALLKEF SKSTRLYGIT KAATVAQFHS RQYQLPKICW LRASAWIYPS AVLTLGSIAF
HAYASGQEEE DSWRPPFRKD LPTFRAEEVK LHNEKSRQLW VTFRGGVYDI TEFVDVHPGG
KIIMQAVGGP LEPHWQRYNF HKQEDVYSML EEMRIGNLHP DDVADAIHDC DKVSEEANPG
YMPKLHPSMD VKSVQPLNAE TGTGELVESF LTPNELFFKR NHHAIPTVDE HSYKLKVSGV
GLQEQEFTLE DLKSKFQPVS VVVTLQCAGN RRQDFNVVKP VRGLQWGPGA IGNAKWTGAL
LIDVLKQAGF ESIVENGVQH VQFTGLDDNG TGEPYGASIP IDVAMKRSNQ VILAYSMNDK
PIPVEHGFPV RVVVPGVVGA RSVKWLSSIV LSKDESPSQW QQSDYKTFHP STDWPTANFS
TVQAIQELPV QSAICSPAEN SSFPRGTKTI AVKGYAWSGG GRDILRVEVS ADNGNTWHSA
VLHLHIQERR NARFAWTLWT CEVPVEDNSG PITLLCKATD SSHNCQPESP NSIWNIRGLV
NNSWHKMPLE GAIKQLRTGQ SYSNFWFHIV AVWTLRSCSS SPFKSQADGP FQSRFRSAEI
VLHRLCPPND RPVHCLLQTC VQSVGFQSPP HVSPCRCIVP SLTLWRLLGQ VKIVVFITCQ
SV
//