UBA4_DEBHA
ID UBA4_DEBHA Reviewed; 448 AA.
AC Q6BHZ2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
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};
GN OrderedLocusNames=DEHA2G14696g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382139; CAG90669.1; -; Genomic_DNA.
DR RefSeq; XP_462179.1; XM_462179.1.
DR AlphaFoldDB; Q6BHZ2; -.
DR SMR; Q6BHZ2; -.
DR STRING; 4959.XP_462179.1; -.
DR EnsemblFungi; CAG90669; CAG90669; DEHA2G14696g.
DR GeneID; 2905098; -.
DR KEGG; dha:DEHA2G14696g; -.
DR VEuPathDB; FungiDB:DEHA2G14696g; -.
DR eggNOG; KOG2017; Eukaryota.
DR HOGENOM; CLU_013325_1_2_1; -.
DR InParanoid; Q6BHZ2; -.
DR OMA; GTIGAMQ; -.
DR OrthoDB; 1445129at2759; -.
DR UniPathway; UPA00988; -.
DR Proteomes; UP000000599; Chromosome G.
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..448
FT /note="Adenylyltransferase and sulfurtransferase UBA4"
FT /id="PRO_0000369225"
FT DOMAIN 349..446
FT /note="Rhodanese"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT ACT_SITE 236
FT /note="Glycyl thioester intermediate; for
FT adenylyltransferase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT ACT_SITE 405
FT /note="Cysteine persulfide intermediate; for
FT sulfurtransferase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 116..120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 133
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 177..178
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 219
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 297
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 300
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
SQ SEQUENCE 448 AA; 50139 MW; 221BE2F637300977 CRC64;
MNDLSREDLL QKIRLLELEN AKLKESKSAV STVSDQYEYD AKYPKIDEYF SSDEYKRYGR
QMIVPQFGSL ISQVKLKKSK VLFIGAGGLG CPALLYLSAS GVGEIGIIDD DLVDISNLHR
QVLHTTESVG IHKCESAKRY INKLNPHVKV NTYPFRLSND NAFDIIEKYD LILDCTDTPA
TRYLINDVSV ICGKTIVSGS GLKTDGQLSI LNFHGIGPCY RCFYPKPPSP GSVTSCSDGG
VVGPAIGLIG ITMALEAIKV ITDFYTDETF KPFLSMYSGY PQQQIRVFKM RNKQANCAVC
GNNPTVLKST ISDNDIDYAE FCGRVNPNVL APELRISVQE YHNYINSSQG ENSILIDVRP
KEQYEITKLP NSINIAWDPT FIKADNIDSY LPSNFDKNTN TFVMCRYGND SQMATKKLIE
NFGFNEVKDI KGGINKWSKE IDSKIPQY
