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G2LZH4 (G2LZH4_9XANT) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 17. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Acetyl-coenzyme A synthetase HAMAP-Rule MF_01123

Short name=AcCoA synthetase HAMAP-Rule MF_01123
Short name=Acs HAMAP-Rule MF_01123
EC=6.2.1.1 HAMAP-Rule MF_01123
Alternative name(s):
Acetate--CoA ligase HAMAP-Rule MF_01123
Acyl-activating enzyme HAMAP-Rule MF_01123
Gene names
Name:acsA HAMAP-Rule MF_01123 EMBL AEO44285.1
ORF Names:XACM_4049 EMBL AEO44285.1
OrganismXanthomonas axonopodis pv. citrumelo F1 [Complete proteome] EMBL AEO44285.1
Taxonomic identifier981368 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Protein attributes

Sequence length672 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA By similarity. HAMAP-Rule MF_01123

Catalytic activity

ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA. HAMAP-Rule MF_01123

Cofactor

Magnesium By similarity. HAMAP-Rule MF_01123

Post-translational modification

Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme By similarity. HAMAP-Rule MF_01123

Sequence similarities

Belongs to the ATP-dependent AMP-binding enzyme family. HAMAP-Rule MF_01123

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region435 – 4406Substrate binding By similarity HAMAP-Rule MF_01123

Sites

Active site5411 By similarity HAMAP-Rule MF_01123
Metal binding5611Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5631Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5661Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Binding site3351Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3591Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site4111Substrate; via nitrogen amide By similarity HAMAP-Rule MF_01123
Binding site5241Substrate By similarity HAMAP-Rule MF_01123
Binding site5391Substrate By similarity HAMAP-Rule MF_01123
Binding site5471Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site5501Substrate By similarity HAMAP-Rule MF_01123
Binding site6081Coenzyme A By similarity HAMAP-Rule MF_01123

Amino acid modifications

Modified residue6331N6-acetyllysine By similarity HAMAP-Rule MF_01123

Sequences

Sequence LengthMass (Da)Tools
G2LZH4 [UniParc].

Last modified November 16, 2011. Version 1.
Checksum: C64B5C7E0CC4FDCF

FASTA67273,981
        10         20         30         40         50         60 
MRHTDCLPRA AATPSSDKFI ASEGAMADVY PVDPAFAADA RVTREQYAAL YRESIEHPEQ 

        70         80         90        100        110        120 
FWGKAAQRLE WFKQPTQIKD VSYALDDFHI RWFGDGELNA SVNCLDRQLA TRGDKTALLF 

       130        140        150        160        170        180 
EPDSPDAQSY PVTYRELYER VCKLGNALRN LGVKKGDRVT IYLPMIVDAA VAMLACARIG 

       190        200        210        220        230        240 
AVHSVVFGGF AANSIADRVI DCQSKLIITA DEGLRGGKKI PLKANVDAAL KIPGTDTVET 

       250        260        270        280        290        300 
VLVVRHTGGA VEMQAPRDRW FHDVVDGQPA ECTPERMNAE DPLFILYTSG STGKPKGVLH 

       310        320        330        340        350        360 
TTAGYLLFAS YTHEVVFDLR EDDIYWCTAD VGWVTGHSYI VYGPLANGAT AVMFEGVPNY 

       370        380        390        400        410        420 
PNVSRFWEVI DKHQVTIFYT APTAIRALMR DGAEPVKKTS RKSLRLLGSV GEPINPEAWR 

       430        440        450        460        470        480 
WYYEVVGDSR CPIVDTWWQT ETGGILISPL AGAVDLKPGS ATLPFFGVQP ALVDAEGKIL 

       490        500        510        520        530        540 
EGATEGNLVL LDSWPGQMRS VYGDHQRFID TYFRTYPGSY FTGDGCRRDA DGYYWITGRV 

       550        560        570        580        590        600 
DDVINVSGHR IGTAEVESAL VSHPKVAEAA VVGFPHDVKG QGIYAYVTLI AGQSPSEDLH 

       610        620        630        640        650        660 
KELVSWVRKE IGPIASPDHL QWAPGLPKTR SGKIMRRILR KIAENAPDQL GDTSTLADPS 

       670 
VVDSLVNERL AR 

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References

[1]"Comparative Genomic Analysis of Xanthomonas axonopodis pv. citrumelo F1, Which Causes Citrus Bacterial Spot Disease, and Related Strains Provides Insights into Virulence and Host Specificity."
Jalan N., Aritua V., Kumar D., Yu F., Jones J.B., Graham J.H., Setubal J.C., Wang N.
J. Bacteriol. 193:6342-6357(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: F1 EMBL AEO44285.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002914 Genomic DNA. Translation: AEO44285.1.
RefSeqYP_004853583.1. NC_016010.1.

3D structure databases

ProteinModelPortalG2LZH4.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEO44285; AEO44285; XACM_4049.
GeneID11131323.
KEGGxax:XACM_4049.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01895.

Enzyme and pathway databases

BioCycXALF981368:GH9H-4049-MONOMER.

Family and domain databases

HAMAPMF_01123. Ac_CoA_synth.
InterProIPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
TIGRFAMsTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameG2LZH4_9XANT
AccessionPrimary (citable) accession number: G2LZH4
Entry history
Integrated into UniProtKB/TrEMBL: November 16, 2011
Last sequence update: November 16, 2011
Last modified: June 11, 2014
This is version 17 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)