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G2LZH4

- G2LZH4_9XANT

UniProt

G2LZH4 - G2LZH4_9XANT

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Protein
Acetyl-coenzyme A synthetase
Gene
acsA, XACM_4049
Organism
Xanthomonas axonopodis pv. citrumelo F1
Status
Unreviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA.UniRule annotation

Cofactori

Magnesium By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei335 – 3351Coenzyme A By similarityUniRule annotation
Binding sitei359 – 3591Coenzyme A By similarityUniRule annotation
Binding sitei411 – 4111Substrate; via nitrogen amide By similarityUniRule annotation
Binding sitei524 – 5241Substrate By similarityUniRule annotation
Binding sitei539 – 5391Substrate By similarityUniRule annotation
Active sitei541 – 5411 By similarityUniRule annotation
Binding sitei547 – 5471Coenzyme A By similarityUniRule annotation
Binding sitei550 – 5501Substrate By similarityUniRule annotation
Metal bindingi561 – 5611Magnesium; via carbonyl oxygen By similarityUniRule annotation
Metal bindingi563 – 5631Magnesium; via carbonyl oxygen By similarityUniRule annotation
Metal bindingi566 – 5661Magnesium; via carbonyl oxygen By similarityUniRule annotation
Binding sitei608 – 6081Coenzyme A By similarityUniRule annotation

GO - Molecular functioni

  1. AMP binding Source: InterPro
  2. ATP binding Source: UniProtKB-KW
  3. acetate-CoA ligase activity Source: UniProtKB-HAMAP
  4. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. acetyl-CoA biosynthetic process from acetate Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

LigaseUniRule annotation

Keywords - Ligandi

ATP-bindingUniRule annotation, MagnesiumUniRule annotation, Metal-bindingUniRule annotation, Nucleotide-binding

Enzyme and pathway databases

BioCyciXALF981368:GH9H-4049-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-coenzyme A synthetaseUniRule annotation (EC:6.2.1.1UniRule annotation)
Short name:
AcCoA synthetaseUniRule annotation
Short name:
AcsUniRule annotation
Alternative name(s):
Acetate--CoA ligase
Acyl-activating enzyme
Gene namesi
Name:acsAUniRule annotationImported
ORF Names:XACM_4049Imported
OrganismiXanthomonas axonopodis pv. citrumelo F1Imported
Taxonomic identifieri981368 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas
ProteomesiUP000001276: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei633 – 6331N6-acetyllysine By similarityUniRule annotation

Post-translational modificationi

Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme By similarity.UniRule annotation

Keywords - PTMi

AcetylationUniRule annotation

Structurei

3D structure databases

ProteinModelPortaliG2LZH4.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni435 – 4406Substrate binding By similarityUniRule annotation

Sequence similaritiesi

Phylogenomic databases

KOiK01895.

Family and domain databases

HAMAPiMF_01123. Ac_CoA_synth.
InterProiIPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

G2LZH4-1 [UniParc]FASTAAdd to Basket

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MRHTDCLPRA AATPSSDKFI ASEGAMADVY PVDPAFAADA RVTREQYAAL    50
YRESIEHPEQ FWGKAAQRLE WFKQPTQIKD VSYALDDFHI RWFGDGELNA 100
SVNCLDRQLA TRGDKTALLF EPDSPDAQSY PVTYRELYER VCKLGNALRN 150
LGVKKGDRVT IYLPMIVDAA VAMLACARIG AVHSVVFGGF AANSIADRVI 200
DCQSKLIITA DEGLRGGKKI PLKANVDAAL KIPGTDTVET VLVVRHTGGA 250
VEMQAPRDRW FHDVVDGQPA ECTPERMNAE DPLFILYTSG STGKPKGVLH 300
TTAGYLLFAS YTHEVVFDLR EDDIYWCTAD VGWVTGHSYI VYGPLANGAT 350
AVMFEGVPNY PNVSRFWEVI DKHQVTIFYT APTAIRALMR DGAEPVKKTS 400
RKSLRLLGSV GEPINPEAWR WYYEVVGDSR CPIVDTWWQT ETGGILISPL 450
AGAVDLKPGS ATLPFFGVQP ALVDAEGKIL EGATEGNLVL LDSWPGQMRS 500
VYGDHQRFID TYFRTYPGSY FTGDGCRRDA DGYYWITGRV DDVINVSGHR 550
IGTAEVESAL VSHPKVAEAA VVGFPHDVKG QGIYAYVTLI AGQSPSEDLH 600
KELVSWVRKE IGPIASPDHL QWAPGLPKTR SGKIMRRILR KIAENAPDQL 650
GDTSTLADPS VVDSLVNERL AR 672
Length:672
Mass (Da):73,981
Last modified:November 16, 2011 - v1
Checksum:iC64B5C7E0CC4FDCF
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP002914 Genomic DNA. Translation: AEO44285.1.
RefSeqiWP_014091438.1. NC_016010.1.
YP_004853583.1. NC_016010.1.

Genome annotation databases

EnsemblBacteriaiAEO44285; AEO44285; XACM_4049.
GeneIDi11131323.
KEGGixax:XACM_4049.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP002914 Genomic DNA. Translation: AEO44285.1 .
RefSeqi WP_014091438.1. NC_016010.1.
YP_004853583.1. NC_016010.1.

3D structure databases

ProteinModelPortali G2LZH4.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AEO44285 ; AEO44285 ; XACM_4049 .
GeneIDi 11131323.
KEGGi xax:XACM_4049.

Phylogenomic databases

KOi K01895.

Enzyme and pathway databases

BioCyci XALF981368:GH9H-4049-MONOMER.

Family and domain databases

HAMAPi MF_01123. Ac_CoA_synth.
InterProi IPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view ]
Pfami PF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEi PS00455. AMP_BINDING. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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 [LARGE SCALE GENOMIC DNA].
    Strain: F1Imported.

Entry informationi

Entry nameiG2LZH4_9XANT
AccessioniPrimary (citable) accession number: G2LZH4
Entry historyi
Integrated into UniProtKB/TrEMBL: November 16, 2011
Last sequence update: November 16, 2011
Last modified: September 3, 2014
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome

External Data

Dasty 3

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