Reviewed, UniProtKB/Swiss-Prot Q9PMD2 (ACSA_CAMJE)

Names and origin

Protein names

Recommended name:
    Acetyl-coenzyme A synthetase
    EC=6.2.1.1
Alternative name(s):
    Acetate--CoA ligase
    Acyl-activating enzyme

Gene names

Name:	acsA
Synonyms:	acs
Ordered Locus Names:	Cj1537c

Organism

Campylobacter jejuni [Complete proteome] [HAMAP]

Taxonomic identifier

197 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length	657 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA. HAMAP MF_01123
Post-translational modification	Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme By similarity.
Sequence similarities	Belongs to the ATP-dependent AMP-binding enzyme family.

Ontologies

Keywords
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Acetylation
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	AMP binding Inferred from electronic annotation. Source: InterPro ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acetate-CoA ligase activity Inferred from electronic annotation. Source: HAMAP protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
fliM	Q0PC73	1	EBI-1194945,EBI-1191095

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 657	657	Acetyl-coenzyme A synthetase HAMAP MF_01123		PRO_0000208358
Sites
	Active site	521	1	By similarity
Amino acid modifications
	Modified residue	617	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9PMD2-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: F1E77BA491B3D0F5	FASTA	657	73,958
	10 20 30 40 50 60 MLNQNNQELF KPSKEFSRNA RIKNLCEYYD LCDEAKEDFE GFWKRQAFEK IEWFSPFSRV 70 80 90 100 110 120 LNEDKAPFYK WFEGGTLNVS YQCLDRHMKT RRNKAALIFE GEMGDYEVYT YRRLLHETCK 130 140 150 160 170 180 AANLLKKFGV KKGDRVVIYM PMIPETAIVM LACARIGAIH SVVFGGFSPE ALRDRIIDAG 190 200 210 220 230 240 AKLVVTADGA FRRGKPYMLK PAVDKALSEG CESVEKVLIV IRNNEPIEYI KGRDYVYNEL 250 260 270 280 290 300 VKNESYKCEP EIMDSEDLLF LLYTSGSTGK PKGVMHASAG YILWAQMTME WVFDIKDYDN 310 320 330 340 350 360 YWCSADVGWI TGHTYVVYGP LACGATTIMH EGTPTYPNSG RWWRMIEEYQ ISKFYTSPTA 370 380 390 400 410 420 IRMLHADAPN EPRKYDLSTL EVLGTVGEPI NPSAWKWFYD EIGGTKSPIV DTWWQTETGG 430 440 450 460 470 480 HMITPLPGAT PLKPGCATLP LPGIFAEVID EEGNKKDEGE DGLLCITKPW PSMIRGIWGN 490 500 510 520 530 540 DERYIESYFS QAKKDGKAVY FSGDGAFYDK NGYITITGRT DDVVNVAGHR IGTAEIESAI 550 560 570 580 590 600 AKHPSVAESA VVSILDTIKG ESLFAFVVLS PASSCDLGGA IETLKELNDI LRVEIGPIAK 610 620 630 640 650 IEKILYTPGL PKTRSGKIMR RILRTIARGE EIKQDISTLE DSKVVETIVK LAKAEFE

References

[1]

"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences." Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. , van Vliet A.H.M., Whitehead S., Barrell B.G. Nature 403:665-668(2000) [PubMed: 10688204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 11168 / Serotype O:2.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL111168 Genomic DNA. Translation: CAL35637.1.
PIR	G81300.
RefSeq	YP_002344909.1.
3D structure databases
HSSP	HSSP built from PDB template 1PG4 based on UniProtKB Q8ZKF6.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9PMD2. 35 interactions.
Genome annotation databases
GeneID	905819.
GenomeReviews	Gene locus Cj1537c in contig AL111168_GR.
KEGG	cje:Cj1537c.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	Q9PMD2. ATYLEWY.
Enzyme and pathway databases
BioCyc	CJEJ192222:CJ1537C-MON.
BRENDA	6.2.1.1. 255835.
Family and domain databases
HAMAP	MF_01123. [Tree]
InterPro	IPR011904. Ac_CoA_lig_AcsA. IPR000873. AMP-dep_Synth/Lig. [Graphical view]
Pfam	PF00501. AMP-binding. 1 hit. [Graphical view]
TIGRFAMs	TIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITE	PS00455. AMP_BINDING. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACSA_CAMJE

Accession

Primary (citable) accession number: Q9PMD2
Secondary accession number(s): Q0P888

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2003
Last sequence update:	October 1, 2000
Last modified:	June 16, 2009
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)