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Protein

Acetyltransferase Pat

Gene

Rv0998

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: -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
  • transferase activity, transferring acyl groups Source: CACAO

Keywordsi

Molecular functionAcyltransferase, Transferase
LigandMagnesium, Metal-binding

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

Phylogenomic databases

eggNOGiENOG410870F Bacteria
COG0454 LUCA
COG0664 LUCA
HOGENOMiHOG000053442
OMAiLDHFVFV

Family and domain databases

CDDicd00038 CAP_ED, 1 hit
Gene3Di2.60.120.10, 1 hit
InterProiView protein in InterPro
IPR016181 Acyl_CoA_acyltransferase
IPR018490 cNMP-bd-like
IPR018488 cNMP-bd_CS
IPR000595 cNMP-bd_dom
IPR000182 GNAT_dom
IPR014710 RmlC-like_jellyroll
PfamiView protein in Pfam
PF13302 Acetyltransf_3, 1 hit
PF00027 cNMP_binding, 1 hit
SMARTiView protein in SMART
SM00100 cNMP, 1 hit
SUPFAMiSSF51206 SSF51206, 1 hit
SSF55729 SSF55729, 1 hit
PROSITEiView protein in PROSITE
PS00889 CNMP_BINDING_2, 1 hit
PS50042 CNMP_BINDING_3, 1 hit
PS51186 GNAT, 1 hit

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, NZ_KK339370.1

Genome annotation databases

EnsemblBacteriaiCCP43748; CCP43748; Rv0998
GeneIDi885385
KEGGimtu:Rv0998
mtv:RVBD_0998
PATRICifig|83332.111.peg.1109

Similar proteinsi

Entry informationi

Entry nameiPAT_MYCTU
AccessioniPrimary (citable) accession number: O05581
Secondary accession number(s): F2GHE2, L0T851
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 28, 2012
Last sequence update: August 1, 1998
Last modified: May 23, 2018
This is version 110 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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