MOCS3_DROPE
ID MOCS3_DROPE Reviewed; 451 AA.
AC B4GKQ3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
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 AltName: Full=Ubiquitin activating enzyme 4 {ECO:0000250|UniProtKB:Q9VLJ8};
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=Uba4 {ECO:0000250|UniProtKB:Q9VLJ8}; ORFNames=GL26133;
OS Drosophila persimilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7234;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSH-3 / Tucson 14011-0111.49;
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
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 -!- 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; CH479184; EDW37219.1; -; Genomic_DNA.
DR RefSeq; XP_002019023.1; XM_002018987.1.
DR AlphaFoldDB; B4GKQ3; -.
DR SMR; B4GKQ3; -.
DR STRING; 7234.FBpp0190240; -.
DR EnsemblMetazoa; FBtr0191748; FBpp0190240; FBgn0163715.
DR GeneID; 6593981; -.
DR KEGG; dpe:6593981; -.
DR eggNOG; KOG2017; Eukaryota.
DR HOGENOM; CLU_013325_1_2_1; -.
DR OMA; GTIGAMQ; -.
DR PhylomeDB; B4GKQ3; -.
DR UniPathway; UPA00344; -.
DR UniPathway; UPA00988; -.
DR Proteomes; UP000008744; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0019008; C:molybdopterin synthase complex; IEA:EnsemblMetazoa.
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:0004792; F:thiosulfate sulfurtransferase activity; ISS:UniProtKB.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; ISS:UniProtKB.
DR GO; GO:0032324; P:molybdopterin cofactor biosynthetic process; IEA:EnsemblMetazoa.
DR GO; GO:0032447; P:protein urmylation; IEA:EnsemblMetazoa.
DR GO; GO:0002143; P:tRNA wobble position uridine thiolation; IEA:InterPro.
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 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Metal-binding; Molybdenum cofactor biosynthesis;
KW Multifunctional enzyme; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transferase; tRNA processing; Zinc.
FT CHAIN 1..451
FT /note="Adenylyltransferase and sulfurtransferase MOCS3"
FT /id="PRO_0000369206"
FT DOMAIN 353..449
FT /note="Rhodanese"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT REGION 42..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 246
FT /note="Glycyl thioester intermediate; for
FT adenylyltransferase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT ACT_SITE 408
FT /note="Cysteine persulfide intermediate; for
FT sulfurtransferase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 127..131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 144
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 188..189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 304
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 307
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT MOD_RES 60
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 451 AA; 50085 MW; 31F81D0BF77BC90C CRC64;
MIDSEALESE RVKLKRDIAD LRANLNRKEQ CLRELEAAIA AGEDSDEAEE SSNDMPTPQT
KLTNDDIARY SRQLILQDFG VQGQLKLKNS SVLIVGMGGL GCPAAQYLVA AGCGHLGLID
YDEVERSNLH RQILHSEHRC GMSKAESARI ALLELNSHCQ IRCHSRLINS MNAMHIIRPY
DVVLDCSDNV ATRYLLNDAC VMLRKPLVSG SALKMDGQLT VYGYGQGPCY RCIYPVPPPP
EAVTNCGDGG VLGAVTGIIG AMQALEAIKV IIGLGDVMSG RLLIFDGSSF MFRNIRIRTK
RPNCHVCSAQ PLITELIDYE MFCGMHATDK DNPLDLLEPD QRLEVKEYHQ KLQSQPHLLL
DVRPPAEFEI CQLPRSINVP LSEILDDSYL KRFAKQLEDK ELPIVLLCRR GNDSQIAAQH
IKNRFPAHSI RDLVGGLHAW TGSVDATFPI Y
