UBA4_PICST
ID UBA4_PICST Reviewed; 443 AA.
AC A3LQF9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Adenylyltransferase and sulfurtransferase UBA4 {ECO:0000255|HAMAP-Rule:MF_03049};
DE AltName: Full=Ubiquitin-like protein activator 4 {ECO:0000255|HAMAP-Rule:MF_03049};
DE Includes:
DE RecName: Full=Adenylyltransferase UBA4 {ECO:0000255|HAMAP-Rule:MF_03049};
DE EC=2.7.7.- {ECO:0000255|HAMAP-Rule:MF_03049};
DE Includes:
DE RecName: Full=Sulfurtransferase UBA4 {ECO:0000255|HAMAP-Rule:MF_03049};
DE EC=2.8.1.- {ECO:0000255|HAMAP-Rule:MF_03049};
GN Name=UBA4 {ECO:0000255|HAMAP-Rule:MF_03049}; ORFNames=PICST_81395;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(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). Acts
CC by mediating the C-terminal thiocarboxylation of sulfur carrier URM1.
CC Its N-terminus first activates URM1 as acyl-adenylate (-COAMP), then
CC the persulfide sulfur on the catalytic cysteine is transferred to URM1
CC to form thiocarboxylation (-COSH) of its C-terminus. The reaction
CC probably involves hydrogen sulfide that is generated from the
CC persulfide intermediate and that acts as nucleophile towards URM1.
CC Subsequently, a transient disulfide bond is formed. Does not use
CC thiosulfate as sulfur donor; NFS1 probably acting as a sulfur donor for
CC thiocarboxylation reactions. Prior mcm(5) tRNA modification by the
CC elongator complex is required for 2-thiolation. May also be involved in
CC protein urmylation. {ECO:0000255|HAMAP-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 -!- 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; CP000496; ABN65201.2; -; Genomic_DNA.
DR RefSeq; XP_001383230.2; XM_001383193.1.
DR AlphaFoldDB; A3LQF9; -.
DR SMR; A3LQF9; -.
DR STRING; 4924.XP_001383230.2; -.
DR EnsemblFungi; ABN65201; ABN65201; PICST_81395.
DR GeneID; 4837270; -.
DR KEGG; pic:PICST_81395; -.
DR eggNOG; KOG2017; Eukaryota.
DR HOGENOM; CLU_013325_1_2_1; -.
DR InParanoid; A3LQF9; -.
DR OMA; GTIGAMQ; -.
DR OrthoDB; 1445129at2759; -.
DR UniPathway; UPA00988; -.
DR Proteomes; UP000002258; Chromosome 2.
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:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IEA:InterPro.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR GO; GO:0032447; P:protein urmylation; 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 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Metal-binding; Multifunctional enzyme;
KW Nucleotide-binding; Reference proteome; Transferase; tRNA processing;
KW Ubl conjugation pathway; Zinc.
FT CHAIN 1..443
FT /note="Adenylyltransferase and sulfurtransferase UBA4"
FT /id="PRO_0000369232"
FT DOMAIN 343..441
FT /note="Rhodanese"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT ACT_SITE 231
FT /note="Glycyl thioester intermediate; for
FT adenylyltransferase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT ACT_SITE 400
FT /note="Cysteine persulfide intermediate; for
FT sulfurtransferase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 83
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 111..115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 172..173
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 217
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 292
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
SQ SEQUENCE 443 AA; 49820 MW; 0A4326D22EA87C14 CRC64;
MAETNSREEE LLRRIQELEL ENEVLKKKVA EVEYDAKYPK IDENFCLDEY KRYGRQMIVP
EFGSLKSQIK LKNSSILVVG AGGLGCPALL YLSAAGIGKI GIVDDDIVDI SNLHRQVLHT
TDSIGMFKCD SAKKYICKLN PHVIVKTYPV RLHNDNAFDI VNDYDIVLDC TDTPAIRYLI
NDVSVLCRKT IVSGSGLKSD GQLSILNFNN EGPCYRCFYP KPPSAESITT CSDGGVIGPC
IGLLGVSMAV ETIKVLTGFY TKDNFKPFLS MYTGYPQQSF RVFKMRGRSD KCSVCGSFPT
VSKEAILNNE IDYVAFCGKV DSNVLTPEDR ITVQQFSDIV TRQSKAPVLL DVRTKEQFQI
AKLPNSINIE WDPTFKKLES LDKYLPEDFD KDTDPVFVVC RYGNDSQLAT RKMKQELDFK
NAKDIIGGLN KWSDIVNPKF PKY
