UBAA_HALVD
ID UBAA_HALVD Reviewed; 270 AA.
AC D4GSF3;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=SAMP-activating enzyme E1;
DE EC=2.7.7.-;
DE AltName: Full=Ubiquitin-like activating enzyme of archaea;
DE Short=Ubl-activating enzyme;
GN Name=ubaA; OrderedLocusNames=HVO_0558;
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
RN [2]
RP SAMPYLATION AT LYS-113, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20054389; DOI=10.1038/nature08659;
RA Humbard M.A., Miranda H.V., Lim J.M., Krause D.J., Pritz J.R., Zhou G.,
RA Chen S., Wells L., Maupin-Furlow J.A.;
RT "Ubiquitin-like small archaeal modifier proteins (SAMPs) in Haloferax
RT volcanii.";
RL Nature 463:54-60(2010).
RN [3]
RP FUNCTION, ACTIVE SITE, MUTAGENESIS OF CYS-188, AND DISRUPTION PHENOTYPE.
RC STRAIN=DS2 / DS70;
RX PubMed=21368171; DOI=10.1073/pnas.1018151108;
RA Miranda H.V., Nembhard N., Su D., Hepowit N., Krause D.J., Pritz J.R.,
RA Phillips C., Soll D., Maupin-Furlow J.A.;
RT "E1- and ubiquitin-like proteins provide a direct link between protein
RT conjugation and sulfur transfer in archaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:4417-4422(2011).
RN [4]
RP FUNCTION.
RC STRAIN=DS2 / DS70;
RX PubMed=24097257; DOI=10.1074/mcp.m113.029652;
RA Miranda H.V., Antelmann H., Hepowit N., Chavarria N.E., Krause D.J.,
RA Pritz J.R., Basell K., Becher D., Humbard M.A., Brocchieri L.,
RA Maupin-Furlow J.A.;
RT "Archaeal ubiquitin-like SAMP3 is isopeptide-linked to proteins via a UbaA-
RT dependent mechanism.";
RL Mol. Cell. Proteomics 13:220-239(2014).
RN [5]
RP FUNCTION, AND INTERACTION WITH NCSA.
RC STRAIN=DS2 / DS70 {ECO:0000303|PubMed:24906001};
RX PubMed=24906001; DOI=10.1371/journal.pone.0099104;
RA Chavarria N.E., Hwang S., Cao S., Fu X., Holman M., Elbanna D.,
RA Rodriguez S., Arrington D., Englert M., Uthandi S., Soell D.,
RA Maupin-Furlow J.A.;
RT "Archaeal Tuc1/Ncs6 homolog required for wobble uridine tRNA thiolation is
RT associated with ubiquitin-proteasome, translation, and RNA processing
RT system homologs.";
RL PLoS ONE 9:e99104-e99104(2014).
CC -!- FUNCTION: Likely activates multiple ubiquitin-like SAMPs for protein
CC conjugation as well as for sulfur transfer, via ATP-dependent
CC adenylation at their C-terminus (PubMed:21368171, PubMed:24097257,
CC PubMed:24906001). In fact, it is required for the formation of all
CC three SAMP1-, SAMP2- and SAMP3-protein conjugates, and for molybdenum
CC cofactor (MoCo) biosynthesis and thiolation of tRNAs (PubMed:21368171,
CC PubMed:24097257). {ECO:0000269|PubMed:21368171,
CC ECO:0000269|PubMed:24097257, ECO:0000269|PubMed:24906001}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[small archaeal modifier protein]-C-terminal Gly-Gly + ATP +
CC H(+) = [small archaeal modifier protein]-C-terminal Gly-Gly-AMP +
CC diphosphate; Xref=Rhea:RHEA:56100, Rhea:RHEA-COMP:14381, Rhea:RHEA-
CC COMP:14383, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:90618, ChEBI:CHEBI:90778;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Interacts with NcsA. {ECO:0000269|PubMed:24906001}.
CC -!- PTM: Sampylated at Lys-113 with the archaeal ubiquitin-like protein
CC SAMP2. Also sampylated with SAMP1. {ECO:0000269|PubMed:20054389}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are deficient in
CC sampylation, i.e. SAMP-protein conjugates. Moreover, they do not grow
CC anaerobically with DMSO and do not show DMSO reductase activity, but
CC their growth in the presence of oxygen is not affected; however, they
CC are retarded in aerobic growth at 50 degrees Celsius. The lysine tRNAs
CC of the mutant strain appear to be nonthiolated.
CC {ECO:0000269|PubMed:21368171}.
CC -!- SIMILARITY: Belongs to the HesA/MoeB/ThiF family. {ECO:0000305}.
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DR EMBL; CP001956; ADE04227.1; -; Genomic_DNA.
DR RefSeq; WP_004044375.1; NZ_AOHU01000098.1.
DR AlphaFoldDB; D4GSF3; -.
DR SMR; D4GSF3; -.
DR STRING; 309800.C498_15935; -.
DR EnsemblBacteria; ADE04227; ADE04227; HVO_0558.
DR GeneID; 8925734; -.
DR KEGG; hvo:HVO_0558; -.
DR eggNOG; arCOG01676; Archaea.
DR HOGENOM; CLU_013325_10_0_2; -.
DR OMA; MIYDALE; -.
DR OrthoDB; 86909at2157; -.
DR BioCyc; MetaCyc:MON-20239; -.
DR BRENDA; 2.7.7.100; 2561.
DR BRENDA; 6.2.1.55; 2561.
DR Proteomes; UP000008243; Chromosome.
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-KW.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IMP:UniProtKB.
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; PF00899; ThiF; 1.
DR SUPFAM; SSF69572; SSF69572; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Isopeptide bond; Metal-binding; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; Thioester bond; Transferase;
KW Ubl conjugation; Zinc.
FT CHAIN 1..270
FT /note="SAMP-activating enzyme E1"
FT /id="PRO_0000397107"
FT ACT_SITE 188
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000305|PubMed:21368171"
FT BINDING 42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 70..74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 131..132
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 248
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT CROSSLNK 113
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SAMP2)"
FT MUTAGEN 188
FT /note="C->S: Loss of activity since this mutant is not able
FT to complement a ubaA deletion in trans to restore
FT sampylation and tRNA thiolation."
FT /evidence="ECO:0000269|PubMed:21368171"
SQ SEQUENCE 270 AA; 28704 MW; B9DFDCD37024FA32 CRC64;
MTLSLDATQL DRYSRHIIMD EVGPEGQGRL LSSRVVVVGA GGLGAPAIQY LAAVGVGELV
VVDDDVVERS NLQRQVVHCD DDVGTPKAES AAAFVRGLNP DVSVEPVEAR VDKSNVHEVV
AGSDVVVDAS DNFPTRYLLN DVCRFEGIPL VHGAIYKFEG QATTLVPDGP CYRCLFPEAP
EPGTVPDCAT TGVLGVLPGT VGCIQATEAM KLLLDEGEAL DGRLLFYDAM DMTFETVPYR
TNPDCPVCGE GGVDSIEDID YVESCAISLD
