ID MOC31_MAIZE Reviewed; 468 AA.
AC B6TNK6; B4FZ31;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Adenylyltransferase and sulfurtransferase MOCS3-1 {ECO:0000255|HAMAP-Rule:MF_03049};
DE AltName: Full=Molybdenum cofactor synthesis protein 3-1 {ECO:0000255|HAMAP-Rule:MF_03049};
DE Includes:
DE RecName: Full=Molybdopterin-synthase adenylyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_03049};
DE EC=2.7.7.80 {ECO:0000255|HAMAP-Rule:MF_03049};
DE AltName: Full=Adenylyltransferase MOCS3-1 {ECO:0000255|HAMAP-Rule:MF_03049};
DE AltName: Full=Sulfur carrier protein MOCS2A adenylyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_03049};
DE Includes:
DE RecName: Full=Molybdopterin-synthase sulfurtransferase 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_03049};
DE AltName: Full=Sulfurtransferase MOCS3-1 {ECO:0000255|HAMAP-Rule:MF_03049};
GN Name=MOCS3-1 {ECO:0000255|HAMAP-Rule:MF_03049};
GN Synonyms=CNX5 {ECO:0000255|HAMAP-Rule:MF_03049},
GN UBA4-1 {ECO:0000255|HAMAP-Rule:MF_03049};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=18937034; DOI=10.1007/s11103-008-9415-4;
RA Alexandrov N.N., Brover V.V., Freidin S., Troukhan M.E., Tatarinova T.V.,
RA Zhang H., Swaller T.J., Lu Y.-P., Bouck J., Flavell R.B., Feldmann K.A.;
RT "Insights into corn genes derived from large-scale cDNA sequencing.";
RL Plant Mol. Biol. 69:179-194(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. B73;
RA Yu Y., Currie J., Lomeli R., Angelova A., Collura K., Wissotski M.,
RA Campos D., Kudrna D., Golser W., Ashely E., Haller K., Descour A.,
RA Fernandes J., Zuccolo A., Soderlund C., Walbot V.;
RT "Maize full-length cDNA project.";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
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;
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=B6TNK6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=B6TNK6-2; Sequence=VSP_036807;
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; EU966571; ACG38689.1; -; mRNA.
DR EMBL; BT042369; ACF87374.1; -; mRNA.
DR AlphaFoldDB; B6TNK6; -.
DR SMR; B6TNK6; -.
DR STRING; 4577.B6TNK6; -.
DR PaxDb; 4577-GRMZM2G160842_P02; -.
DR eggNOG; KOG2017; Eukaryota.
DR InParanoid; B6TNK6; -.
DR UniPathway; UPA00344; -.
DR UniPathway; UPA00988; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; B6TNK6; baseline and differential.
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: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 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.
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..468
FT /note="Adenylyltransferase and sulfurtransferase MOCS3-1"
FT /id="PRO_0000369213"
FT DOMAIN 371..466
FT /note="Rhodanese"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT ACT_SITE 258
FT /note="Glycyl thioester intermediate; for
FT adenylyltransferase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT ACT_SITE 426
FT /note="Cysteine persulfide intermediate; for
FT sulfurtransferase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 132
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 139..143
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 156
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 200..201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 244
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 316
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 319
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT VAR_SEQ 167..191
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_036807"
FT CONFLICT 445
FT /note="T -> A (in Ref. 2; ACF87374)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 468 AA; 50275 MW; 116AE9D55839605C CRC64;
MGGRREAIER ELKKLRAERE ELDGRIRLLE SQLEAGPAGF NGAAAGKGVG DDACGGSGAC
QSRVGNEFAP DGSLPADMIY RYSRHLLLPD FGVEGQRKLS QSSILVVGAG GLGSPLALYL
AACGVGRLGI VDGDDVELNN LHRQIIHKEA YVGQSKVKSA ADACREINSS IKVVEYHHTL
KPCNALEVAR KYDIVVDATD NLPTRYMISD CCVLLNKPLV SGAALGLEGQ LTVYHHNGSP
CYRCLFPTPP PVAACQRCSD SGVLGVVPGV IGCLQALEAI KVATGVGEPL CGRMLLFDAL
SARIRVVKLR GSSPDCTHCG ENSVFTEEDF QKFDYESFTQ SPMSDKAAPS VNVLPESARI
TCREYKKLAD DGEPHLLLDV RPAHHFQIAS ISPSHNIPLS MLEEKLPALE ASLKEAGEGS
ALVVLCRRGN DSQRAVQLLR EKGFTSAKDI IGGLQAWGRD VDPDFPVY
//
