ID A0A194PDN4_PAPXU Unreviewed; 830 AA.
AC A0A194PDN4;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Molybdenum cofactor sulfurase {ECO:0000256|HAMAP-Rule:MF_03050};
DE Short=MCS {ECO:0000256|HAMAP-Rule:MF_03050};
DE Short=MOS {ECO:0000256|HAMAP-Rule:MF_03050};
DE Short=MoCo sulfurase {ECO:0000256|HAMAP-Rule:MF_03050};
DE EC=2.8.1.9 {ECO:0000256|HAMAP-Rule:MF_03050};
DE AltName: Full=Molybdenum cofactor sulfurtransferase {ECO:0000256|HAMAP-Rule:MF_03050};
DE AltName: Full=Protein maroon-like {ECO:0000256|HAMAP-Rule:MF_03050};
DE Short=Ma-l {ECO:0000256|HAMAP-Rule:MF_03050};
GN Name=mal {ECO:0000256|HAMAP-Rule:MF_03050};
GN ORFNames=RR46_14871 {ECO:0000313|EMBL:KPI91367.1};
OS Papilio xuthus (Asian swallowtail butterfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Papilionidae; Papilioninae; Papilio.
OX NCBI_TaxID=66420 {ECO:0000313|EMBL:KPI91367.1, ECO:0000313|Proteomes:UP000053268};
RN [1] {ECO:0000313|EMBL:KPI91367.1, ECO:0000313|Proteomes:UP000053268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ya'a_city_454_Px {ECO:0000313|EMBL:KPI91367.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KPI91367.1};
RX PubMed=26354079; DOI=10.1038/ncomms9212;
RA Li X., Fan D., Zhang W., Liu G., Zhang L., Zhao L., Fang X., Chen L.,
RA Dong Y., Chen Y., Ding Y., Zhao R., Feng M., Zhu Y., Feng Y., Jiang X.,
RA Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., Kronforst M.R.,
RA Wang W.;
RT "Outbred genome sequencing and CRISPR/Cas9 gene editing in butterflies.";
RL Nat. Commun. 6:8212-8212(2015).
CC -!- FUNCTION: Sulfurates the molybdenum cofactor. Sulfation of molybdenum
CC is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase
CC (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and
CC 1 sulfur atom in active form. {ECO:0000256|HAMAP-Rule:MF_03050}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + L-cysteine + Mo-molybdopterin = A + H2O + L-alanine +
CC thio-Mo-molybdopterin; Xref=Rhea:RHEA:42636, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:35235,
CC ChEBI:CHEBI:57972, ChEBI:CHEBI:71302, ChEBI:CHEBI:82685; EC=2.8.1.9;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03050};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_03050};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. MOCOS subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_03050}.
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DR EMBL; KQ459606; KPI91367.1; -; Genomic_DNA.
DR RefSeq; XP_013165019.1; XM_013309565.1.
DR RefSeq; XP_013165020.1; XM_013309566.1.
DR RefSeq; XP_013165021.1; XM_013309567.1.
DR RefSeq; XP_013165022.1; XM_013309568.1.
DR RefSeq; XP_013165023.1; XM_013309569.1.
DR AlphaFoldDB; A0A194PDN4; -.
DR STRING; 66420.A0A194PDN4; -.
DR GeneID; 106115917; -.
DR KEGG; pxu:106115917; -.
DR OrthoDB; 448292at2759; -.
DR Proteomes; UP000053268; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008265; F:Mo-molybdopterin cofactor sulfurase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0102867; F:molybdenum cofactor sulfurtransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR HAMAP; MF_03050; MOCOS; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR005302; MoCF_Sase_C.
DR InterPro; IPR028886; MoCo_sulfurase.
DR InterPro; IPR005303; MOCOS_middle.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR PANTHER; PTHR14237:SF19; MOLYBDENUM COFACTOR SULFURASE; 1.
DR PANTHER; PTHR14237; MOLYBDOPTERIN COFACTOR SULFURASE MOSC; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR Pfam; PF03473; MOSC; 1.
DR Pfam; PF03476; MOSC_N; 1.
DR SUPFAM; SSF141673; MOSC N-terminal domain-like; 1.
DR SUPFAM; SSF50800; PK beta-barrel domain-like; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS51340; MOSC; 1.
PE 3: Inferred from homology;
KW Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150,
KW ECO:0000256|HAMAP-Rule:MF_03050};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_03050}; Reference proteome {ECO:0000313|Proteomes:UP000053268};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03050}.
FT DOMAIN 655..822
FT /note="MOSC"
FT /evidence="ECO:0000259|PROSITE:PS51340"
FT ACT_SITE 417
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03050"
FT MOD_RES 250
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03050"
SQ SEQUENCE 830 AA; 94597 MW; 732D2669E716C73E CRC64;
MSETTTLSRV IDSEQMQAIT SEFNRLGERC YLEHAGAALY PQSLLQHVHE DLLNNVYMNP
HTDKYTRDCI EQIRCLVLNH FHTDPSKYSI IFTSGATQSL KLTVESFEFS SNTEEGFECG
SFVYLNENHT SVLGLREIAE DKNVDVINIS HDNFLKSIKQ NHPAPSGQKS KTDGNILLAY
PAKSNFNGFK YPLDCIQNIK NGCLNRYLMK HLCKVNCNWY VLLDAAAYVP TNNLDLSITQ
PDFVCLSFYK IFGYPTGLGA LLVKNTSADV LCKKRYFGGG TVDIVISGEN FHIKRKILHE
RMEDGTLPFL SILALKHCFD MLHRLIPKTI NNHIMDTISH HTFYLAKDLY NQLNELHHPN
GKKAVVLYMD SDFSDIKIQG GIVTFNLLRE DGSFVGFMEF QNMADLFNIN VRTGCFCNSG
SCQRHLNTSN REMKEMYKAG HKCGDEIDLI NGNPTGAIRV SFGYYNTFND VDKLVLMVCR
CFVRTVFKKP KRTMTCLQEL SVYKPVKKAY KEGMIKLLNE RSYFNGYDIL PETPLESSDI
ILDEIAIFPI KSCGAFKIKT SWKIGLKGFE YDREWMIIRE NGVCLTQKQS TQMCMIKPEI
DLKRKLLILH FKGKPSISVP LEPIIENKTK FASMCTSKVC MDMVKGYDCG DDVSDWISNA
LGISFLRLIK QSSTDVRPQK KNADGEQKLL SLCNQAQFLL INKASVRWLH GRIKDPMFSA
TVDNLTDRFR GNLIIDRAVE LTEREWHRII IGKHEFKVDG PCQRCHMICI DQQTGEKTAE
PLRTISEQFA GKMRFGIYLS YVGPVNGMKD KALKVNSIVK PMINEDDISR
//
