MOCS3_MOUSE
ID MOCS3_MOUSE Reviewed; 460 AA.
AC A2BDX3;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Adenylyltransferase and sulfurtransferase MOCS3 {ECO:0000255|HAMAP-Rule:MF_03049};
DE AltName: Full=Molybdenum cofactor synthesis protein 3 {ECO:0000255|HAMAP-Rule:MF_03049};
DE Includes:
DE RecName: Full=Molybdopterin-synthase adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_03049};
DE EC=2.7.7.80 {ECO:0000255|HAMAP-Rule:MF_03049};
DE AltName: Full=Adenylyltransferase MOCS3 {ECO:0000255|HAMAP-Rule:MF_03049};
DE AltName: Full=Sulfur carrier protein MOCS2A adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_03049};
DE Includes:
DE RecName: Full=Molybdopterin-synthase sulfurtransferase {ECO:0000255|HAMAP-Rule:MF_03049};
DE EC=2.8.1.11 {ECO:0000255|HAMAP-Rule:MF_03049};
DE AltName: Full=Sulfur carrier protein MOCS2A sulfurtransferase {ECO:0000255|HAMAP-Rule:MF_03049};
DE AltName: Full=Sulfurtransferase MOCS3 {ECO:0000255|HAMAP-Rule:MF_03049};
GN Name=Mocs3; Synonyms=Uba4;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Spleen, and Testis;
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: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA
CC wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also
CC essential during biosynthesis of the molybdenum cofactor. Acts by
CC mediating the C-terminal thiocarboxylation of sulfur carriers URM1 and
CC MOCS2A. Its N-terminus first activates URM1 and MOCS2A as acyl-
CC adenylates (-COAMP), then the persulfide sulfur on the catalytic
CC cysteine is transferred to URM1 and MOCS2A to form thiocarboxylation (-
CC COSH) of their C-terminus. The reaction probably involves hydrogen
CC sulfide that is generated from the persulfide intermediate and that
CC acts as nucleophile towards URM1 and MOCS2A. Subsequently, a transient
CC disulfide bond is formed. Does not use thiosulfate as sulfur donor;
CC NFS1 probably acting as a sulfur donor for thiocarboxylation reactions.
CC {ECO:0000255|HAMAP-Rule:MF_03049}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[molybdopterin-synthase sulfur-carrier protein]-C-terminal
CC Gly-Gly + ATP + H(+) = [molybdopterin-synthase sulfur-carrier
CC protein]-C-terminal Gly-Gly-AMP + diphosphate; Xref=Rhea:RHEA:43616,
CC Rhea:RHEA-COMP:12159, Rhea:RHEA-COMP:12202, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:90618,
CC ChEBI:CHEBI:90778; EC=2.7.7.80; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03049};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[molybdopterin-synthase sulfur-carrier protein]-C-terminal
CC Gly-Gly-AMP + AH2 + S-sulfanyl-L-cysteinyl-[cysteine desulfurase] =
CC [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-NH-
CC CH2-C(O)SH + A + AMP + H(+) + L-cysteinyl-[cysteine desulfurase];
CC Xref=Rhea:RHEA:48612, Rhea:RHEA-COMP:12157, Rhea:RHEA-COMP:12158,
CC Rhea:RHEA-COMP:12159, Rhea:RHEA-COMP:12160, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:61963, ChEBI:CHEBI:90618, ChEBI:CHEBI:90619,
CC ChEBI:CHEBI:456215; EC=2.8.1.11; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03049};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03049};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03049};
CC -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03049}.
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03049}.
CC -!- SUBUNIT: Interacts with NFS1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03049}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the HesA/MoeB/ThiF
CC family. UBA4 subfamily. {ECO:0000255|HAMAP-Rule:MF_03049}.
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DR EMBL; BX005039; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS50802.1; -.
DR RefSeq; NP_001153802.1; NM_001160330.1.
DR AlphaFoldDB; A2BDX3; -.
DR SMR; A2BDX3; -.
DR IntAct; A2BDX3; 1.
DR STRING; 10090.ENSMUSP00000096670; -.
DR iPTMnet; A2BDX3; -.
DR PhosphoSitePlus; A2BDX3; -.
DR SwissPalm; A2BDX3; -.
DR EPD; A2BDX3; -.
DR MaxQB; A2BDX3; -.
DR PaxDb; A2BDX3; -.
DR PeptideAtlas; A2BDX3; -.
DR PRIDE; A2BDX3; -.
DR ProteomicsDB; 290289; -.
DR Antibodypedia; 28627; 190 antibodies from 24 providers.
DR Ensembl; ENSMUST00000099071; ENSMUSP00000096670; ENSMUSG00000074576.
DR GeneID; 69372; -.
DR KEGG; mmu:69372; -.
DR UCSC; uc012cjs.1; mouse.
DR CTD; 27304; -.
DR MGI; MGI:1916622; Mocs3.
DR VEuPathDB; HostDB:ENSMUSG00000074576; -.
DR eggNOG; KOG2017; Eukaryota.
DR GeneTree; ENSGT00940000160847; -.
DR HOGENOM; CLU_013325_1_2_1; -.
DR InParanoid; A2BDX3; -.
DR OMA; GTIGAMQ; -.
DR OrthoDB; 1445129at2759; -.
DR PhylomeDB; A2BDX3; -.
DR TreeFam; TF106103; -.
DR Reactome; R-MMU-947581; Molybdenum cofactor biosynthesis.
DR UniPathway; UPA00344; -.
DR UniPathway; UPA00988; -.
DR BioGRID-ORCS; 69372; 25 hits in 72 CRISPR screens.
DR ChiTaRS; Mocs3; mouse.
DR PRO; PR:A2BDX3; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; A2BDX3; protein.
DR Bgee; ENSMUSG00000074576; Expressed in seminiferous tubule of testis and 201 other tissues.
DR Genevisible; A2BDX3; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061605; F:molybdopterin-synthase adenylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0061604; F:molybdopterin-synthase sulfurtransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016779; F:nucleotidyltransferase activity; ISS:UniProtKB.
DR GO; GO:0016783; F:sulfurtransferase activity; ISS:UniProtKB.
DR GO; GO:0004792; F:thiosulfate sulfurtransferase activity; ISS:UniProtKB.
DR GO; GO:0042292; F:URM1 activating enzyme activity; ISS:UniProtKB.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; ISS:UniProtKB.
DR GO; GO:0032447; P:protein urmylation; IBA:GO_Central.
DR GO; GO:0034227; P:tRNA thio-modification; ISS:UniProtKB.
DR GO; GO:0002143; P:tRNA wobble position uridine thiolation; IBA:GO_Central.
DR GO; GO:0002098; P:tRNA wobble uridine modification; ISS:UniProtKB.
DR Gene3D; 3.40.250.10; -; 1.
DR HAMAP; MF_03049; MOCS3_Uba4; 1.
DR InterPro; IPR028885; MOCS3/Uba4.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR10953; PTHR10953; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR Pfam; PF00899; ThiF; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF69572; SSF69572; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Disulfide bond; Metal-binding;
KW Molybdenum cofactor biosynthesis; Multifunctional enzyme;
KW Nucleotide-binding; Reference proteome; Transferase; tRNA processing; Zinc.
FT CHAIN 1..460
FT /note="Adenylyltransferase and sulfurtransferase MOCS3"
FT /id="PRO_0000281918"
FT DOMAIN 347..458
FT /note="Rhodanese"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT ACT_SITE 239
FT /note="Glycyl thioester intermediate; for
FT adenylyltransferase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT ACT_SITE 412
FT /note="Cysteine persulfide intermediate; for
FT sulfurtransferase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 113
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 120..124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 137
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 181..182
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 297
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 300
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT DISULFID 316..324
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
SQ SEQUENCE 460 AA; 49375 MW; 7340FD4B2D9826F1 CRC64;
MAAPEDVAAL QAEITRREEE LASLKRRLAA ALTAEPEPER PLRVPPPPLA PRAALSRDEI
LRYSRQLLLP ELGVRGQLRL AAAAVLVVGC GGLGCPLAQY LAAAGVGRLG LVDHDVVETS
NLARQVLHGE AQAGESKARS AAAALRRLNS AVECVAYPRA LAEDWALDLV RGYDVVADCC
DNVPTRYLVN DACVLAGRPL VSASALRFEG QMTVYHHDGG PCYRCVFPRP PPPETVTNCA
DGGVLGAVPG VLGCAQALEV LKIAAGLGSS YSGSMLLFDG LGGHFRRIRL RRRRPDCVVC
GQQPTVTRLQ DYEAFCGSSA TDKCRALKLL CPEERISVTD YKRLLDSGAP HVLLDVRPQV
EVDICRLPHS LHIPLSQLER RDADSLKLLG AALRKGKQES QEGVALPVYV ICKLGNDSQK
AVKVLQSLTA VPELDSLTVQ DIVGGLMAWA AKIDGTFPQY
