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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)DescriptionActionsGraphical viewLength
Binding sitei138cAMPCombined sources1 Publication1
Binding sitei173Substrate1 Publication1
Metal bindingi214Magnesium1 Publication1
Binding sitei277Substrate1 Publication1
Binding sitei286Substrate1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi88 – 91cAMPCombined sources1 Publication4
Nucleotide bindingi98 – 99cAMPCombined sources1 Publication2

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

BioCyciMTBH37RV:G185E-5156-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)DescriptionActionsGraphical viewLength
Mutagenesisi173H → K: Induces autoacetylation of the new lysine in the absence of cAMP. 1 Publication1
Mutagenesisi184R → A: Completely abolishes the interaction with the aliphatic tail of the substrate lysine. 1 Publication1
Mutagenesisi185F → A: Completely abolishes the interaction with the aliphatic tail of the substrate lysine. 1 Publication1
Mutagenesisi223R → 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 Publication1
Mutagenesisi225V → A: Substantially decreases the interaction with the aliphatic tail of the substrate lysine. 1 Publication1
Mutagenesisi237A → V: Completely abolishes the interaction with the aliphatic tail of the substrate lysine. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004203621 – 333Acetyltransferase PatAdd BLAST333

Proteomic databases

PaxDbiO05581.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi83332.Rv0998.

Structurei

Secondary structure

1333
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi12 – 15Combined sources4
Helixi19 – 21Combined sources3
Helixi26 – 35Combined sources10
Beta strandi37 – 41Combined sources5
Beta strandi46 – 48Combined sources3
Beta strandi57 – 62Combined sources6
Beta strandi65 – 70Combined sources6
Beta strandi76 – 81Combined sources6
Beta strandi86 – 88Combined sources3
Helixi89 – 94Combined sources6
Beta strandi99 – 106Combined sources8
Beta strandi108 – 113Combined sources6
Helixi115 – 123Combined sources9
Helixi127 – 142Combined sources16
Beta strandi146 – 149Combined sources4
Beta strandi155 – 160Combined sources6
Helixi166 – 168Combined sources3
Beta strandi171 – 173Combined sources3
Helixi178 – 182Combined sources5
Helixi183 – 185Combined sources3
Helixi193 – 202Combined sources10
Beta strandi205 – 214Combined sources10
Beta strandi217 – 226Combined sources10
Beta strandi233 – 240Combined sources8
Helixi242 – 244Combined sources3
Helixi249 – 263Combined sources15
Beta strandi268 – 274Combined sources7
Helixi278 – 285Combined sources8
Turni286 – 288Combined sources3
Beta strandi292 – 295Combined sources4
Beta strandi298 – 304Combined sources7
Turni308 – 310Combined sources3
Beta strandi311 – 313Combined sources3
Helixi315 – 330Combined sources16

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini156 – 318N-acetyltransferasePROSITE-ProRule annotationAdd BLAST163

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni238 – 240Substrate binding1 Publication3
Regioni246 – 251Substrate binding1 Publication6

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.

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4AVAX-ray1.70A1-333[»]
4AVBX-ray1.80A/B1-333[»]
4AVCX-ray2.81A/B1-333[»]
ProteinModelPortaliO05581.
SMRiO05581.
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.

Enzyme and pathway databases

BioCyciMTBH37RV:G185E-5156-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...

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: November 2, 2016
This is version 104 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.