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Protein

Acetyltransferase Pat

Gene

Rv0998

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes specifically the acetylation of the epsilon-amino group of a highly conserved lysine residue in acetyl-CoA synthetase (ACS). This acetylation results in the inactivation of ACS activity and could be important for mycobacteria to adjust to environmental changes.3 Publications

Cofactori

Mg2+1 Publication

Enzyme regulationi

Autoinhibited and allosterically activated by 3,5-cyclic adenosine monophosphate (cAMP). An extensive conformational rearrangement relieves this autoinhibition by means of a substrate-mimicking lid that covers the protein-substrate binding surface.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei138 – 1381cAMPCombined sources1 Publication
Binding sitei173 – 1731Substrate1 Publication
Metal bindingi214 – 2141Magnesium1 Publication
Binding sitei277 – 2771Substrate1 Publication
Binding sitei286 – 2861Substrate1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi88 – 914cAMPCombined sources1 Publication
Nucleotide bindingi98 – 992cAMPCombined sources1 Publication

GO - Molecular functioni

  • acetyltransferase activity Source: MTBBASE
  • cAMP binding Source: MTBBASE
  • metal ion binding Source: UniProtKB-KW
  • N-acetyltransferase activity Source: InterPro
  • transferase activity, transferring acyl groups Source: CACAO
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMTBRV:RV0998-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyltransferase Pat (EC:2.3.1.-)
Alternative name(s):
GCN5-like enzyme
GCN5-related N-acetyltransferase
Short name:
GNAT
Protein acetyltransferase
Short name:
Pat
Gene namesi
Ordered Locus Names:Rv0998
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv0998.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi173 – 1731H → K: Induces autoacetylation of the new lysine in the absence of cAMP. 1 Publication
Mutagenesisi184 – 1841R → A: Completely abolishes the interaction with the aliphatic tail of the substrate lysine. 1 Publication
Mutagenesisi185 – 1851F → A: Completely abolishes the interaction with the aliphatic tail of the substrate lysine. 1 Publication
Mutagenesisi223 – 2231R → A: Substantially decreases the interaction with the aliphatic tail of the substrate lysine. Markedly reduced activity, with an altered pH-rate profile and abolishes direct interactions with R-184. 1 Publication
Mutagenesisi225 – 2251V → A: Substantially decreases the interaction with the aliphatic tail of the substrate lysine. 1 Publication
Mutagenesisi237 – 2371A → V: Completely abolishes the interaction with the aliphatic tail of the substrate lysine. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 333333Acetyltransferase PatPRO_0000420362Add
BLAST

Proteomic databases

PaxDbiO05581.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi83332.Rv0998.

Structurei

Secondary structure

1
333
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi12 – 154Combined sources
Helixi19 – 213Combined sources
Helixi26 – 3510Combined sources
Beta strandi37 – 415Combined sources
Beta strandi46 – 483Combined sources
Beta strandi57 – 626Combined sources
Beta strandi65 – 706Combined sources
Beta strandi76 – 816Combined sources
Beta strandi86 – 883Combined sources
Helixi89 – 946Combined sources
Beta strandi99 – 1068Combined sources
Beta strandi108 – 1136Combined sources
Helixi115 – 1239Combined sources
Helixi127 – 14216Combined sources
Beta strandi146 – 1494Combined sources
Beta strandi155 – 1606Combined sources
Helixi166 – 1683Combined sources
Beta strandi171 – 1733Combined sources
Helixi178 – 1825Combined sources
Helixi183 – 1853Combined sources
Helixi193 – 20210Combined sources
Beta strandi205 – 21410Combined sources
Beta strandi217 – 22610Combined sources
Beta strandi233 – 2408Combined sources
Helixi242 – 2443Combined sources
Helixi249 – 26315Combined sources
Beta strandi268 – 2747Combined sources
Helixi278 – 2858Combined sources
Turni286 – 2883Combined sources
Beta strandi292 – 2954Combined sources
Beta strandi298 – 3047Combined sources
Turni308 – 3103Combined sources
Beta strandi311 – 3133Combined sources
Helixi315 – 33016Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4AVAX-ray1.70A1-333[»]
4AVBX-ray1.80A/B1-333[»]
4AVCX-ray2.81A/B1-333[»]
ProteinModelPortaliO05581.
SMRiO05581. Positions 8-333.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini156 – 318163N-acetyltransferasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni238 – 2403Substrate binding1 Publication
Regioni246 – 2516Substrate binding1 Publication

Sequence similaritiesi

Contains 1 cyclic nucleotide-binding domain.PROSITE-ProRule annotation
Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410870F. Bacteria.
COG0454. LUCA.
COG0664. LUCA.
HOGENOMiHOG000053442.
OMAiGWVGGRE.
OrthoDBiEOG6GTZM5.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR018490. cNMP-bd-like.
IPR018488. cNMP-bd_CS.
IPR000595. cNMP-bd_dom.
IPR000182. GNAT_dom.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
PfamiPF13302. Acetyltransf_3. 1 hit.
PF00027. cNMP_binding. 1 hit.
[Graphical view]
SMARTiSM00100. cNMP. 1 hit.
[Graphical view]
SUPFAMiSSF51206. SSF51206. 1 hit.
SSF55729. SSF55729. 1 hit.
PROSITEiPS00889. CNMP_BINDING_2. 1 hit.
PS50042. CNMP_BINDING_3. 1 hit.
PS51186. GNAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O05581-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDGIAELTGA RVEDLAGMDV FQGCPAEGLV SLAASVQPLR AAAGQVLLRQ
60 70 80 90 100
GEPAVSFLLI SSGSAEVSHV GDDGVAIIAR ALPGMIVGEI ALLRDSPRSA
110 120 130 140 150
TVTTIEPLTG WTGGRGAFAT MVHIPGVGER LLRTARQRLA AFVSPIPVRL
160 170 180 190 200
ADGTQLMLRP VLPGDRERTV HGHIQFSGET LYRRFMSARV PSPALMHYLS
210 220 230 240 250
EVDYVDHFVW VVTDGSDPVA DARFVRDETD PTVAEIAFTV ADAYQGRGIG
260 270 280 290 300
SFLIGALSVA ARVDGVERFA ARMLSDNVPM RTIMDRYGAV WQREDVGVIT
310 320 330
TMIDVPGPGE LSLGREMVDQ INRVARQVIE AVG
Length:333
Mass (Da):35,626
Last modified:August 1, 1998 - v2
Checksum:iF66AFCDF3247331D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP43748.1.
PIRiA70602.
RefSeqiNP_215513.1. NC_000962.3.
WP_003405164.1. NC_000962.3.

Genome annotation databases

EnsemblBacteriaiCCP43748; CCP43748; Rv0998.
GeneIDi885385.
KEGGimtu:Rv0998.
mtv:RVBD_0998.
PATRICi18150746. VBIMycTub87468_1113.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP43748.1.
PIRiA70602.
RefSeqiNP_215513.1. NC_000962.3.
WP_003405164.1. NC_000962.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4AVAX-ray1.70A1-333[»]
4AVBX-ray1.80A/B1-333[»]
4AVCX-ray2.81A/B1-333[»]
ProteinModelPortaliO05581.
SMRiO05581. Positions 8-333.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv0998.

Proteomic databases

PaxDbiO05581.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP43748; CCP43748; Rv0998.
GeneIDi885385.
KEGGimtu:Rv0998.
mtv:RVBD_0998.
PATRICi18150746. VBIMycTub87468_1113.

Organism-specific databases

TubercuListiRv0998.

Phylogenomic databases

eggNOGiENOG410870F. Bacteria.
COG0454. LUCA.
COG0664. LUCA.
HOGENOMiHOG000053442.
OMAiGWVGGRE.
OrthoDBiEOG6GTZM5.

Enzyme and pathway databases

BioCyciMTBRV:RV0998-MONOMER.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR018490. cNMP-bd-like.
IPR018488. cNMP-bd_CS.
IPR000595. cNMP-bd_dom.
IPR000182. GNAT_dom.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
PfamiPF13302. Acetyltransf_3. 1 hit.
PF00027. cNMP_binding. 1 hit.
[Graphical view]
SMARTiSM00100. cNMP. 1 hit.
[Graphical view]
SUPFAMiSSF51206. SSF51206. 1 hit.
SSF55729. SSF55729. 1 hit.
PROSITEiPS00889. CNMP_BINDING_2. 1 hit.
PS50042. CNMP_BINDING_3. 1 hit.
PS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25618 / H37Rv.
  2. "cAMP-regulated protein lysine acetylases in mycobacteria."
    Nambi S., Basu N., Visweswariah S.S.
    J. Biol. Chem. 285:24313-24323(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  3. "Reversible acetylation and inactivation of Mycobacterium tuberculosis acetyl-CoA synthetase is dependent on cAMP."
    Xu H., Hegde S.S., Blanchard J.S.
    Biochemistry 50:5883-5892(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ATCC 25618 / H37Rv.
  5. "Cyclic AMP regulation of protein lysine acetylation in Mycobacterium tuberculosis."
    Lee H.J., Lang P.T., Fortune S.M., Sassetti C.M., Alber T.
    Nat. Struct. Mol. Biol. 19:811-818(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, CAMP AND MAGNESIUM IONS, FUNCTION, MUTAGENESIS OF HIS-173; ARG-184; PHE-185; ARG-223; VAL-225 AND ALA-237, ENZYME REGULATION, COFACTOR, SUBUNIT.

Entry informationi

Entry nameiPAT_MYCTU
AccessioniPrimary (citable) accession number: O05581
Secondary accession number(s): F2GHE2, L0T851
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2012
Last sequence update: August 1, 1998
Last modified: January 20, 2016
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.