ID MOCS3_ARATH Reviewed; 464 AA. AC Q9ZNW0; B9DGV4; Q058R2; DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 27-MAR-2024, entry version 156. 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 13 {ECO:0000255|HAMAP-Rule:MF_03049}; DE Short=AtStr13; DE AltName: Full=Sulfurtransferase MOCS3 {ECO:0000255|HAMAP-Rule:MF_03049}; GN Name=MOCS3 {ECO:0000255|HAMAP-Rule:MF_03049}; GN Synonyms=CNX5 {ECO:0000255|HAMAP-Rule:MF_03049}, STR13, UBA4 GN {ECO:0000255|HAMAP-Rule:MF_03049}; OrderedLocusNames=At5g55130; GN ORFNames=MCO15.8; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. Columbia; RA Nieder J., Gutzke G., Mendel R.R.; RT "Isolation and sequencing of a genomic region coding for the MPT-synthase- RT sulphurylase (Cnx5) in A.thaliana."; RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC STRAIN=cv. Columbia; RA Nieder J., Stallmeyer B., Brinkmann H., Mendel R.R.; RT "Molybdenum cofactor biosynthesis: identification of A.thaliana cDNAs RT homologous to the E.coli sulfotransferase MoeB."; RL (In) Cram W.J., de Kok L.J., Stulen I., Brunold C., Rennenberg H. (eds.); RL Sulphur Metabolism in Higher Plants, pp.275-277, Backhuys Publishers, RL Leiden (1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=9628582; DOI=10.1093/dnares/5.1.41; RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N., RA Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence RT features of the regions of 1,456,315 bp covered by nineteen physically RT assigned P1 and TAC clones."; RL DNA Res. 5:41-54(1998). RN [4] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RX PubMed=27862469; DOI=10.1111/tpj.13415; RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S., RA Town C.D.; RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference RT genome."; RL Plant J. 89:789-804(2017). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=cv. Columbia; RX PubMed=14993207; DOI=10.1101/gr.1515604; RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M., RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M., RA Weissenbach J., Salanoubat M.; RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a RT combined approach to evaluate and improve Arabidopsis genome annotation."; RL Genome Res. 14:406-413(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=cv. Columbia; TISSUE=Rosette leaf; RX PubMed=19423640; DOI=10.1093/dnares/dsp009; RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., RA Shinozaki K.; RT "Analysis of multiple occurrences of alternative splicing events in RT Arabidopsis thaliana using novel sequenced full-length cDNAs."; RL DNA Res. 16:155-164(2009). RN [7] RP GENE FAMILY. RX PubMed=17408957; DOI=10.1016/j.plaphy.2007.02.005; RA Bartels A., Mock H.P., Papenbrock J.; RT "Differential expression of Arabidopsis sulfurtransferases under various RT growth conditions."; RL Plant Physiol. Biochem. 45:178-187(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 a nucleophile towards URM1 and MOCS2A. Subsequently, a CC transient disulfide bond is formed. Does not use thiosulfate as sulfur CC donor; NFS1 probably acting as a sulfur donor for thiocarboxylation CC reactions. {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; Evidence={ECO:0000255|HAMAP- CC 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 -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9ZNW0-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9ZNW0-2; Sequence=VSP_042632; CC -!- SIMILARITY: In the N-terminal section; belongs to the HesA/MoeB/ThiF CC family. UBA4 subfamily. {ECO:0000255|HAMAP-Rule:MF_03049}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF124160; AAD18051.1; -; Genomic_DNA. DR EMBL; AF124159; AAD18050.1; -; mRNA. DR EMBL; AB010071; BAB08582.1; -; Genomic_DNA. DR EMBL; CP002688; AED96586.1; -; Genomic_DNA. DR EMBL; CP002688; AED96587.1; -; Genomic_DNA. DR EMBL; BT029156; ABJ17091.1; -; mRNA. DR EMBL; AK317295; BAH19971.1; -; mRNA. DR RefSeq; NP_001032076.1; NM_001036999.1. [Q9ZNW0-2] DR RefSeq; NP_200324.1; NM_124895.3. [Q9ZNW0-1] DR AlphaFoldDB; Q9ZNW0; -. DR SMR; Q9ZNW0; -. DR STRING; 3702.Q9ZNW0; -. DR PaxDb; 3702-AT5G55130-1; -. DR ProteomicsDB; 238299; -. [Q9ZNW0-1] DR EnsemblPlants; AT5G55130.1; AT5G55130.1; AT5G55130. [Q9ZNW0-1] DR EnsemblPlants; AT5G55130.2; AT5G55130.2; AT5G55130. [Q9ZNW0-2] DR GeneID; 835604; -. DR Gramene; AT5G55130.1; AT5G55130.1; AT5G55130. [Q9ZNW0-1] DR Gramene; AT5G55130.2; AT5G55130.2; AT5G55130. [Q9ZNW0-2] DR KEGG; ath:AT5G55130; -. DR Araport; AT5G55130; -. DR TAIR; AT5G55130; CNX5. DR eggNOG; KOG2017; Eukaryota. DR HOGENOM; CLU_013325_1_2_1; -. DR InParanoid; Q9ZNW0; -. DR OrthoDB; 53913at2759; -. DR PhylomeDB; Q9ZNW0; -. DR UniPathway; UPA00344; -. DR UniPathway; UPA00988; -. DR PRO; PR:Q9ZNW0; -. DR Proteomes; UP000006548; Chromosome 5. DR ExpressionAtlas; Q9ZNW0; baseline and differential. DR GO; GO:0005829; C:cytosol; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008265; F:Mo-molybdopterin cofactor sulfurase activity; ISS:TAIR. 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:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro. DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0002143; P:tRNA wobble position uridine thiolation; IEA:InterPro. DR CDD; cd01526; RHOD_ThiF; 1. DR CDD; cd00757; ThiF_MoeB_HesA_family; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR Gene3D; 3.40.250.10; Rhodanese-like domain; 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:SF102; ADENYLYLTRANSFERASE AND SULFURTRANSFERASE MOCS3; 1. DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1. DR Pfam; PF00581; Rhodanese; 1. DR Pfam; PF00899; ThiF; 1. DR SMART; SM00450; RHOD; 1. DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1. DR PROSITE; PS50206; RHODANESE_3; 1. DR Genevisible; Q9ZNW0; AT. PE 2: Evidence at transcript level; KW Alternative splicing; ATP-binding; Cytoplasm; Metal-binding; KW Molybdenum cofactor biosynthesis; Multifunctional enzyme; KW Nucleotide-binding; Reference proteome; Transferase; tRNA processing; Zinc. FT CHAIN 1..464 FT /note="Adenylyltransferase and sulfurtransferase MOCS3" FT /id="PRO_0000120584" FT DOMAIN 358..462 FT /note="Rhodanese" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049" FT ACT_SITE 248 FT /note="Glycyl thioester intermediate; for FT adenylyltransferase activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049" FT ACT_SITE 422 FT /note="Cysteine persulfide intermediate; for FT sulfurtransferase activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049" FT BINDING 101 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049" FT BINDING 122 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049" FT BINDING 129..133 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049" FT BINDING 146 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049" FT BINDING 190..191 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049" FT BINDING 231 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049" FT BINDING 234 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049" FT BINDING 306 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049" FT BINDING 309 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049" FT VAR_SEQ 85..111 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:19423640" FT /id="VSP_042632" SQ SEQUENCE 464 AA; 50574 MW; 844C7C35C7737940 CRC64; MMSNGGDSSE IVRELEELKL KKAEIEHRIS TLEAKLQDTA AVELYDAVSN GDSYLTAPEL EHGLSPDQIY RYSRQLLLPS FAVEGQSNLL KSSVLVIGAG GLGSPALLYL AACGVGQLGI IDHDVVELNN MHRQIIHTEA FIGHPKVKSA AAACRSINST IKVDEYVEAL RTSNALEILS QYDIIVDATD NPPSRYMISD CCVLLGKPLV SGAALGMEGQ LTVYNHNGGP CYRCLFPTPP PTSACQRCSD SGVLGVVPGV IGCLQALETI KLASLVGEPL SERMLLFDAL SARMRIVKIR GRSSQCTVCG DNSSFNKQTF KDFDYEDFTQ FPLFAGPLNL LPAESRISSK EFKEILQKKE QHVLLDVRPS HHYKIVSLPD SLNIPLANLE TRLNELTSAL KEKGNGHANT ESCTNPSVFV VCRRGNDSQR AVQYLRESGF DSAKDIIGGL EAWAANVNPN FPTY //