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Q8KBY0

- ACSA_CHLTE

UniProt

Q8KBY0 - ACSA_CHLTE

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Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Chlorobium tepidum (strain ATCC 49652 / DSM 12025 / TLS)
Status
Reviewed - 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

Mg2+UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei323 – 3231Coenzyme AUniRule annotation
Binding sitei347 – 3471Coenzyme AUniRule annotation
Binding sitei512 – 5121ATPUniRule annotation
Binding sitei527 – 5271ATPUniRule annotation
Binding sitei535 – 5351Coenzyme A; via carbonyl oxygenUniRule annotation
Binding sitei538 – 5381ATPUniRule annotation
Metal bindingi549 – 5491Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi551 – 5511Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi554 – 5541Magnesium; via carbonyl oxygenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi399 – 4013ATPUniRule annotation
Nucleotide bindingi423 – 4286ATPUniRule 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

Ligase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciCTEP194439:GHN0-1691-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 annotation
Synonyms:acs
Ordered Locus Names:CT1652
OrganismiChlorobium tepidum (strain ATCC 49652 / DSM 12025 / TLS)
Taxonomic identifieri194439 [NCBI]
Taxonomic lineageiBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobaculum
ProteomesiUP000001007: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 659659Acetyl-coenzyme A synthetasePRO_0000208360Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei621 – 6211N6-acetyllysineUniRule annotation

Post-translational modificationi

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

Keywords - PTMi

Acetylation

Interactioni

Protein-protein interaction databases

STRINGi194439.CT1652.

Structurei

3D structure databases

ProteinModelPortaliQ8KBY0.
SMRiQ8KBY0. Positions 23-656.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni205 – 2084Coenzyme A bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0365.
HOGENOMiHOG000229981.
KOiK01895.
OMAiGGCEAVT.
OrthoDBiEOG68WR2H.

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.

Q8KBY0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MATEQTKGQS SESISSVLSE RRKFPPPEAF SSQSHISSME QYEKLYADAA
60 70 80 90 100
ADPDKYWGDL AEQFHWFKKW DSVLEWNAPY AKWFNGGTTN IAYNCLDVHV
110 120 130 140 150
GSWRKNKAAI IWEGEEGNER ILTYGELHRQ VSKFANVLKI AGIKPGDKVA
160 170 180 190 200
IYMGMVPELV IAVLACARVG AVHNVIFAGF AAHAITERVN DSRAKIVICA
210 220 230 240 250
DGTRRRGSTI NLKNIVDEAI INTPSVKNVI VLKVTGEEIH MHDGMDHWWH
260 270 280 290 300
DLMGLAVDEC EPAQVDSEHP LFLLYTSGST GKPKGILHTT AGYMVHAASS
310 320 330 340 350
FKYVFDIKDE DIYFCTADIG WITGHTYIIY GPLLNGATVF MYEGAPNYPQ
360 370 380 390 400
WDRFWDIINR HKITILYTAP TAIRAFIRAG NEWVTKHDLS SLRLLGTVGE
410 420 430 440 450
PINPEAWMWY HKYVGQEKCP IVDTWWQTET GGIMISPMPG ATPTKPGTAT
460 470 480 490 500
RPLPGIMVDV VRKDGTPCNA NEGGYLVVKR PWPSMLRTIY GDNERYEKTY
510 520 530 540 550
WSEFPGMYFT GDGARKDDDG YIWIMGRVDD VVNVSGHRLG TSEVESALVS
560 570 580 590 600
HEAVAEAAVV SRPDEIKGNA LVAFVTLKDG YEGDAKLRDS LGKHVAKEIG
610 620 630 640 650
AIAKPDEIRW AKGLPKTRSG KIMRRLLREL ATSNEIKGDV TTLEDLGVIE

NLREQEDEG
Length:659
Mass (Da):73,576
Last modified:September 26, 2003 - v2
Checksum:i2BB84C9AB13EA034
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006470 Genomic DNA. Translation: AAM72877.1.
RefSeqiNP_662535.2. NC_002932.3.

Genome annotation databases

EnsemblBacteriaiAAM72877; AAM72877; CT1652.
GeneIDi1006138.
KEGGicte:CT1652.
PATRICi21401177. VBIChlTep116050_1493.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006470 Genomic DNA. Translation: AAM72877.1 .
RefSeqi NP_662535.2. NC_002932.3.

3D structure databases

ProteinModelPortali Q8KBY0.
SMRi Q8KBY0. Positions 23-656.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 194439.CT1652.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAM72877 ; AAM72877 ; CT1652 .
GeneIDi 1006138.
KEGGi cte:CT1652.
PATRICi 21401177. VBIChlTep116050_1493.

Phylogenomic databases

eggNOGi COG0365.
HOGENOMi HOG000229981.
KOi K01895.
OMAi GGCEAVT.
OrthoDBi EOG68WR2H.

Enzyme and pathway databases

BioCyci CTEP194439:GHN0-1691-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 49652 / DSM 12025 / TLS.

Entry informationi

Entry nameiACSA_CHLTE
AccessioniPrimary (citable) accession number: Q8KBY0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: September 26, 2003
Last modified: November 26, 2014
This is version 72 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3