MOCOS_BOVIN
ID MOCOS_BOVIN Reviewed; 882 AA.
AC Q9N0E7; F1N3A9; G3N1I0;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 3.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Molybdenum cofactor sulfurase {ECO:0000255|HAMAP-Rule:MF_03050};
DE Short=MCS {ECO:0000255|HAMAP-Rule:MF_03050};
DE Short=MOS {ECO:0000255|HAMAP-Rule:MF_03050};
DE Short=MoCo sulfurase {ECO:0000255|HAMAP-Rule:MF_03050};
DE EC=2.8.1.9 {ECO:0000255|HAMAP-Rule:MF_03050};
DE AltName: Full=Molybdenum cofactor sulfurtransferase {ECO:0000255|HAMAP-Rule:MF_03050};
GN Name=MOCOS {ECO:0000255|HAMAP-Rule:MF_03050}; Synonyms=MCSU;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INVOLVEMENT IN XU-II, TISSUE
RP SPECIFICITY, VARIANT PRO-193, AND VARIANT XU-II TYR-290 DEL.
RC TISSUE=Liver;
RX PubMed=10801779; DOI=10.1074/jbc.c000230200;
RA Watanabe T., Ihara N., Itoh T., Fujita T., Sugimoto Y.;
RT "Deletion mutation in Droshophila ma-l homologous, putative molybdopterin
RT cofactor sulfurase gene is associated with bovine xanthinuria type II.";
RL J. Biol. Chem. 275:21789-21792(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-133 (ISOFORM 1).
RA Lewin H.A., Soares M.B., Rebeiz M., Pardinas J., Liu L., Larson J.H.;
RT "Bovine ESTs.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
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.
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:0000255|HAMAP-Rule:MF_03050};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03050};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9N0E7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9N0E7-2; Sequence=VSP_036820;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:10801779}.
CC -!- DISEASE: Note=Defects in MOCOS are the cause of xanthinuria type II
CC (XU-II). XU-II is characterized by excretion of very large amounts of
CC xanthine in the urine and a tendency to form xanthine stones. Uric acid
CC is strikingly diminished in serum and urine. In addition, cows
CC suffering of XU-II cannot metabolize allopurinol into oxypurinol due to
CC the lack of ADO activity.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. MOCOS subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_03050}.
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DR EMBL; AB036422; BAA98138.1; -; mRNA.
DR EMBL; DAAA02056390; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BF045807; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_776506.1; NM_174081.2.
DR AlphaFoldDB; Q9N0E7; -.
DR SMR; Q9N0E7; -.
DR STRING; 9913.ENSBTAP00000055724; -.
DR PaxDb; Q9N0E7; -.
DR PRIDE; Q9N0E7; -.
DR Ensembl; ENSBTAT00000048768; ENSBTAP00000045753; ENSBTAG00000012252. [Q9N0E7-2]
DR Ensembl; ENSBTAT00000065375; ENSBTAP00000055724; ENSBTAG00000012252. [Q9N0E7-1]
DR GeneID; 281226; -.
DR KEGG; bta:281226; -.
DR CTD; 55034; -.
DR VEuPathDB; HostDB:ENSBTAG00000012252; -.
DR eggNOG; KOG2142; Eukaryota.
DR GeneTree; ENSGT00940000157051; -.
DR HOGENOM; CLU_010913_0_1_1; -.
DR InParanoid; Q9N0E7; -.
DR OMA; WCLVHQG; -.
DR OrthoDB; 394559at2759; -.
DR TreeFam; TF105761; -.
DR Reactome; R-BTA-947581; Molybdenum cofactor biosynthesis.
DR Proteomes; UP000009136; Chromosome 24.
DR Bgee; ENSBTAG00000012252; Expressed in oviduct epithelium and 101 other tissues.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008265; F:Mo-molybdopterin cofactor sulfurase activity; IMP:UniProtKB.
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 GO; GO:0043545; P:molybdopterin cofactor metabolic process; IMP:UniProtKB.
DR Gene3D; 3.40.640.10; -; 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; MOSC_N.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR Pfam; PF00266; Aminotran_5; 1.
DR Pfam; PF03473; MOSC; 1.
DR Pfam; PF03476; MOSC_N; 1.
DR SUPFAM; SSF50800; SSF50800; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS51340; MOSC; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Molybdenum cofactor biosynthesis; Phosphoprotein;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..882
FT /note="Molybdenum cofactor sulfurase"
FT /id="PRO_0000249951"
FT DOMAIN 707..868
FT /note="MOSC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT REGION 496..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 425
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT MOD_RES 265
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT MOD_RES 528
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96EN8"
FT MOD_RES 530
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96EN8"
FT VAR_SEQ 1..47
FT /note="MAGGAAHPGAELLPFARFLDSSLQPLVYGYGRGTLHELRAREFGRLA -> M
FT QSRQPRALLPRSP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10801779"
FT /id="VSP_036820"
FT VARIANT 193
FT /note="G -> P (requires 2 nucleotide substitutions)"
FT /evidence="ECO:0000269|PubMed:10801779"
FT VARIANT 290
FT /note="Missing (in XU-II)"
FT /evidence="ECO:0000269|PubMed:10801779"
FT CONFLICT 520
FT /note="V -> M (in Ref. 1; BAA98138)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 882 AA; 97205 MW; DFD9E55146E47926 CRC64;
MAGGAAHPGA ELLPFARFLD SSLQPLVYGY GRGTLHELRA REFGRLAGTV YLDHAGTTLF
PQSQITSFMK DLMENVYGNP HSQNISSKLT HDTVEQVRFR ILAHFHTSPE DYTVIFTSGS
TAALKLVAEA FPWVSPGPEG SGSCFCYLTD SHTSVVGMRK ITAAMNVSSI PVRPEDMWSA
ERQDAAAAGD PAGQPPHLFC YPAQSNFSGT RYPLSWIGEV KSGRRRPASR PGKWFVLLDA
AAFVGTSPLD LSVHQADFVP ISFYKIFGFP TGLGALLVNN RLAALLRKTY FGGGTAAAYL
AGDDFYVPRE SVAERFEDGT ISFLDVIALK HGFDALERLT GGMESIRQHT FTLAQYTYTA
LSSLRYPNGA PVVQIYSDSD FSSPEVQGPV ISFNVLDDHG NVVGYSQVDK MASLHNIHVR
TGCFCNTGAC QRHLGISDEM VKKHLQAGHV CGDDVDLIDG QPTGSVRISF GYMSTLEDAQ
AFLRFIIATR LHSSHGQPLP LATPGEAGAP PEDSEAQNAV PAARARGSSS PQEDTSPHSG
VWNNSPTAVD AEGLCPPLLE ATGTQQTTSE KAADVPDGDL RSHVITNLFL YPIKSCAAFE
VIRWPLGSQG LLYDRSWMVV NHNGICLSQK QEPRLCLIQP FIDLQRRIMV IKAQGMEPIE
VPLEENSEQV QICQSKVCAD RVNTYDCGEK ISNWLSKFFG RPYHLIKQSS DFQRNAKKKH
GKDQSAHTTA TLSLVNEAQY LLINRSSILE LQQQLSTSCE NGKEELFPMN NLISRFRANI
ITNGTRAFEE EKWDEISIGS LRFQVLGPCH RCQMICIDQQ TGQRNQDVFQ KLSERRERKV
KFGVYLMHTS LDLSSPCYLS VGSQVLPLLK ENMEHHDIPA TE
