MOCS3_ARATH
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 03-AUG-2022, entry version 149.
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,
GN UBA4 {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 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 -!- 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}.
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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.AT5G55130.1; -.
DR PaxDb; Q9ZNW0; -.
DR PRIDE; Q9ZNW0; -.
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; locus:2161635; AT5G55130.
DR eggNOG; KOG2017; Eukaryota.
DR HOGENOM; CLU_013325_1_2_1; -.
DR InParanoid; Q9ZNW0; -.
DR OrthoDB; 1445129at2759; -.
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 Genevisible; Q9ZNW0; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
DR GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IBA:GO_Central.
DR GO; GO:0042292; F:URM1 activating enzyme activity; IBA:GO_Central.
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 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 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
