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SALTY:LYSAC

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Species (Taxon ID) Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720). (99287)
Gene Name(s) pat (synonyms: yfiQ)
Protein Name(s) Protein lysine acetyltransferase Pat
External Links
UniProt Q8ZMX2
EMBL AE006468
RefSeq NP_461586.1
WP_000082639.1
ProteinModelPortal Q8ZMX2
DIP DIP-61211N
STRING 99287.STM2651
PaxDb Q8ZMX2
PRIDE Q8ZMX2
EnsemblBacteria AAL21545
GeneID 1254174
KEGG stm:STM2651
PATRIC 32383959
eggNOG ENOG4105CD5
COG0454
COG1042
HOGENOM HOG000220090
KO K09181
OMA IVIYMES
PhylomeDB Q8ZMX2
Proteomes UP000001014
GO GO:0005524
GO:0048037
GO:0046872
GO:0008080
Gene3D 3.30.470.20
3.40.50.261
3.40.50.720
3.40.630.30
InterPro IPR016181
IPR011761
IPR013816
IPR003781
IPR000182
IPR016040
IPR032875
IPR016102
Pfam PF00583
PF13380
PF13607
SMART SM00881
SUPFAM SSF51735
SSF52210
SSF55729
PROSITE PS50975
PS51186

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0051591

response to cAMP

PMID:27974467[1]

ECO:0000314

P

Organism: Salmonella enterica (Salmonella typhimurium). Paper's Protein Name: Protein acetyltransferase OR Lysine acetyltransferase (Pat). UniProt's Protein Name: Protein lysine acetyltransferase. "As shown in Fig. 2C, SePat increases the acetylation level of SeAcs Lys609 in vitro (lane 4), and cAMP promotes Pat-dependent acetylation substantially (lane 7). The addition of cAMP to the acetylation assay system further decreases SeAcs activity, suggesting SeAcs acetylation promoted by cAMP also contributes to the inhibitory effect of cAMP on SeAcs."

complete
CACAO 12271

enables

GO:0005524

ATP binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011761
InterPro:IPR013815

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011761

F

Seeded From UniProt

complete

enables

GO:0048037

cofactor binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003781

F

Seeded From UniProt

complete

enables

GO:0016746

transferase activity, transferring acyl groups

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0012

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

enables

GO:0016740

transferase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0808

F

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Han, X et al. (2017) Cyclic AMP Inhibits the Activity and Promotes the Acetylation of Acetyl-CoA Synthetase through Competitive Binding to the ATP/AMP Pocket. J. Biol. Chem. 292 1374-1384 PubMed GONUTS page