ID   MOCOS_MOUSE             Reviewed;         862 AA.
AC   Q14CH1;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 113.
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;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver, and Lung;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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:0000255|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: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   -!- 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; BC113180; AAI13181.1; -; mRNA.
DR   EMBL; BC113786; AAI13787.1; -; mRNA.
DR   CCDS; CCDS37750.1; -.
DR   RefSeq; NP_081055.1; NM_026779.1.
DR   AlphaFoldDB; Q14CH1; -.
DR   SMR; Q14CH1; -.
DR   BioGRID; 212940; 8.
DR   IntAct; Q14CH1; 1.
DR   STRING; 10090.ENSMUSP00000063609; -.
DR   iPTMnet; Q14CH1; -.
DR   PhosphoSitePlus; Q14CH1; -.
DR   EPD; Q14CH1; -.
DR   jPOST; Q14CH1; -.
DR   MaxQB; Q14CH1; -.
DR   PaxDb; Q14CH1; -.
DR   PeptideAtlas; Q14CH1; -.
DR   PRIDE; Q14CH1; -.
DR   ProteomicsDB; 290091; -.
DR   Antibodypedia; 41960; 54 antibodies from 19 providers.
DR   Ensembl; ENSMUST00000068006; ENSMUSP00000063609; ENSMUSG00000039616.
DR   GeneID; 68591; -.
DR   KEGG; mmu:68591; -.
DR   UCSC; uc008egy.1; mouse.
DR   CTD; 55034; -.
DR   MGI; MGI:1915841; Mocos.
DR   VEuPathDB; HostDB:ENSMUSG00000039616; -.
DR   eggNOG; KOG2142; Eukaryota.
DR   GeneTree; ENSGT00940000157051; -.
DR   HOGENOM; CLU_010913_0_1_1; -.
DR   InParanoid; Q14CH1; -.
DR   OMA; WCLVHQG; -.
DR   OrthoDB; 394559at2759; -.
DR   PhylomeDB; Q14CH1; -.
DR   TreeFam; TF105761; -.
DR   Reactome; R-MMU-947581; Molybdenum cofactor biosynthesis.
DR   BioGRID-ORCS; 68591; 2 hits in 73 CRISPR screens.
DR   ChiTaRS; Mocos; mouse.
DR   PRO; PR:Q14CH1; -.
DR   Proteomes; UP000000589; Chromosome 18.
DR   RNAct; Q14CH1; protein.
DR   Bgee; ENSMUSG00000039616; Expressed in granulocyte and 151 other tissues.
DR   Genevisible; Q14CH1; MM.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008265; F:Mo-molybdopterin cofactor sulfurase activity; ISS: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; ISS: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   1: Evidence at protein level;
KW   Molybdenum cofactor biosynthesis; Phosphoprotein; Pyridoxal phosphate;
KW   Reference proteome; Transferase.
FT   CHAIN           1..862
FT                   /note="Molybdenum cofactor sulfurase"
FT                   /id="PRO_0000249953"
FT   DOMAIN          704..855
FT                   /note="MOSC"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT   ACT_SITE        424
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT   MOD_RES         34
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96EN8"
FT   MOD_RES         264
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT   MOD_RES         517
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96EN8"
SQ   SEQUENCE   862 AA;  95013 MW;  E422CF97C6E91878 CRC64;
     MACGAAERGP EPPAFQRHLE ASTQRLAHGY GLRSMSELRD QEFGRLAGTV YLDHAGATLF
     PQSQLTNFTK DLMENVYGNP HSQNITSKLT HDTVEQVRYR ILTHFHTTPE DYIVIFTAGS
     TAALRLVAEA FPWVSRSPEN SGSHFCYLTD NHTSVVGMRK VAAAMSVTSI PVKPEDMWSA
     EGKDAGACDP DCQLPHLFCY PAQSNFSGTR YPLSWVEEVK SGRRSPVNAP GKWFVLLDAA
     SYVSTSPLDL SAHQADFIPI SFYKIFGLPT GLGALLVNKH VAPLLRKGYF GGGTAAAYLA
     GEDFYVPRSS VAERFEDGTI SFLDVIALKH GFDALEHLTG GMVNIQQHTF ALVQYTHSAL
     SSLRYLNGAP VVRIYSDSEF SSPDVQGPII NFNVLDDGGK IIGYSQVDKM ASLYNIHLRT
     GCFCNLGACQ RHLGLSDEMV KKHFQAGHVC GDDVDIIDGR PTGSVRISFG YMSTLEDAQA
     FLRFISTIYL RSPSDQPVPQ ASISDAGALT SKSDCHSPQE GSCTDPSVCN GSYPDTNIMD
     LHPSLSKASS AQQTPQDKAA GILNGDPGSH IVTNIYLYPI KSCAAFEVTK WPVGSQGLLY
     DRSWMVVNHN GICMSQKQEP RLCLIQPFID LQQRIMVIKA EGMEPIQVPL EEDGEQTQIC
     QSRVCADRVN TYDCGENVSR WLSKFLGRLC HLIKQSPHFQ RNARKTPKKG QPPGTTVALS
     LVNEAQYLLV NTSSILELQR QLNASDEHGK EESFSMKDLI SRFRANIITK GARAFEEEKW
     DEISIGSLHF QVLGPCHRCQ MICINQQTGQ RNQDVFQTLS ESRGRKVNFG VYLMHSYLDL
     SSPCFLSVGS EVLPVLKDCG VS