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G2LZH4

- G2LZH4_9XANT

UniProt

G2LZH4 - G2LZH4_9XANT

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Protein

Acetyl-coenzyme A synthetase

Gene

acsA

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.UniRule annotation

Catalytic activityi

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

Cofactori

Note: Magnesium.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei335 – 3351Coenzyme AUniRule annotation
Binding sitei359 – 3591Coenzyme AUniRule annotation
Binding sitei524 – 5241ATPUniRule annotation
Binding sitei539 – 5391ATPUniRule annotation
Binding sitei547 – 5471Coenzyme A; via carbonyl oxygenUniRule annotation
Binding sitei550 – 5501ATPUniRule annotation
Metal bindingi561 – 5611Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi563 – 5631Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi566 – 5661Magnesium; via carbonyl oxygenUniRule annotation
Binding sitei608 – 6081Coenzyme AUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi411 – 4133ATPUniRule annotation
Nucleotide bindingi435 – 4406ATPUniRule annotation

GO - Molecular functioni

  1. acetate-CoA ligase activity Source: UniProtKB-HAMAP
  2. AMP binding Source: InterPro
  3. ATP binding Source: UniProtKB-KW
  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 ligaseUniRule annotation
Acyl-activating enzymeUniRule annotation
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-acetyllysineUniRule annotation

Post-translational modificationi

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

Keywords - PTMi

AcetylationUniRule annotation

Structurei

3D structure databases

ProteinModelPortaliG2LZH4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni215 – 2184Coenzyme A bindingUniRule annotation

Sequence similaritiesi

Belongs to the ATP-dependent AMP-binding enzyme family.UniRule annotation

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

« Hide

        10         20         30         40         50
MRHTDCLPRA AATPSSDKFI ASEGAMADVY PVDPAFAADA RVTREQYAAL
60 70 80 90 100
YRESIEHPEQ FWGKAAQRLE WFKQPTQIKD VSYALDDFHI RWFGDGELNA
110 120 130 140 150
SVNCLDRQLA TRGDKTALLF EPDSPDAQSY PVTYRELYER VCKLGNALRN
160 170 180 190 200
LGVKKGDRVT IYLPMIVDAA VAMLACARIG AVHSVVFGGF AANSIADRVI
210 220 230 240 250
DCQSKLIITA DEGLRGGKKI PLKANVDAAL KIPGTDTVET VLVVRHTGGA
260 270 280 290 300
VEMQAPRDRW FHDVVDGQPA ECTPERMNAE DPLFILYTSG STGKPKGVLH
310 320 330 340 350
TTAGYLLFAS YTHEVVFDLR EDDIYWCTAD VGWVTGHSYI VYGPLANGAT
360 370 380 390 400
AVMFEGVPNY PNVSRFWEVI DKHQVTIFYT APTAIRALMR DGAEPVKKTS
410 420 430 440 450
RKSLRLLGSV GEPINPEAWR WYYEVVGDSR CPIVDTWWQT ETGGILISPL
460 470 480 490 500
AGAVDLKPGS ATLPFFGVQP ALVDAEGKIL EGATEGNLVL LDSWPGQMRS
510 520 530 540 550
VYGDHQRFID TYFRTYPGSY FTGDGCRRDA DGYYWITGRV DDVINVSGHR
560 570 580 590 600
IGTAEVESAL VSHPKVAEAA VVGFPHDVKG QGIYAYVTLI AGQSPSEDLH
610 620 630 640 650
KELVSWVRKE IGPIASPDHL QWAPGLPKTR SGKIMRRILR KIAENAPDQL
660 670
GDTSTLADPS VVDSLVNERL AR
Length:672
Mass (Da):73,981
Last modified:November 16, 2011 - v1
Checksum:iC64B5C7E0CC4FDCF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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: November 26, 2014
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

External Data

Dasty 3