UBA4_CANAL
ID UBA4_CANAL Reviewed; 438 AA.
AC Q59WH7; A0A1D8PF04;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=CAALFM_C110930CA; ORFNames=CaO19.2324, CaO19.9860;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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; CP017623; AOW26719.1; -; Genomic_DNA.
DR RefSeq; XP_713929.1; XM_708836.2.
DR AlphaFoldDB; Q59WH7; -.
DR SMR; Q59WH7; -.
DR STRING; 237561.Q59WH7; -.
DR GeneID; 3644432; -.
DR KEGG; cal:CAALFM_C110930CA; -.
DR CGD; CAL0000183559; UBA4.
DR VEuPathDB; FungiDB:C1_10930C_A; -.
DR eggNOG; KOG2017; Eukaryota.
DR HOGENOM; CLU_013325_1_0_1; -.
DR InParanoid; Q59WH7; -.
DR OrthoDB; 1445129at2759; -.
DR UniPathway; UPA00988; -.
DR PRO; PR:Q59WH7; -.
DR Proteomes; UP000000559; Chromosome 1.
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: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:0032447; P:protein urmylation; IBA:GO_Central.
DR GO; GO:0002143; P:tRNA wobble position uridine thiolation; IBA:GO_Central.
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..438
FT /note="Adenylyltransferase and sulfurtransferase UBA4"
FT /id="PRO_0000369223"
FT DOMAIN 340..436
FT /note="Rhodanese"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT ACT_SITE 229
FT /note="Glycyl thioester intermediate; for
FT adenylyltransferase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT ACT_SITE 396
FT /note="Cysteine persulfide intermediate; for
FT sulfurtransferase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 109..113
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 170..171
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 215
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 290
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
FT BINDING 293
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03049"
SQ SEQUENCE 438 AA; 48867 MW; 06EDAED33592E443 CRC64;
MSEPSKEELL ARIAQLELEN EQLKQQNGKK SQHEQFNKID DNFSLDEYKR YGRQMIVPQF
GSLESQIKLK NSKVLVVGAG GLGSPALLYL SSAGIGKIGI IDPDTVDTSN LHRQVIHNTE
MVGEFKCISA QNYINKLNPH VVVEVYPTAL NNDNAFGIVS QYDLVLDCTD HPAVRYLIND
VCVLLGKTIV SGSGLKSDGQ LTVLNFANSG PCYRCFYPQP PSPDSVTSCS DGGVIGPAIG
LVGVAMAVET IKIITGYYTK DNFVPFLASY SAYPQQQLRV FKMRKRQKDC AVCGENPQIS
QRMIEDGTIN YKTFCGRATF DPIDDKFRVS PKDYDSVVQN KKKHILIDVR PREQFQITHL
PNAINVQWDP TFRKADAIEQ YLPDDSTKDD EIYVVCRFGN DSQLAAKKLI GMGYPNVRDI
IGGLDKWSDD VDSKIPKY
