SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q8KBY0

- ACSA_CHLTE

UniProt

Q8KBY0 - ACSA_CHLTE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Acetyl-coenzyme A synthetase
Gene
acsA, acs, CT1652
Organism
Chlorobium tepidum (strain ATCC 49652 / DSM 12025 / TLS)
Status
Reviewed - Annotation score: 4 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 sitei323 – 3231Coenzyme A By similarity
Binding sitei347 – 3471Coenzyme A By similarity
Binding sitei399 – 3991Substrate; via amide nitrogen By similarity
Binding sitei512 – 5121Substrate By similarity
Binding sitei527 – 5271Substrate By similarity
Active sitei529 – 5291 By similarity
Binding sitei535 – 5351Coenzyme A By similarity
Binding sitei538 – 5381Substrate By similarity
Metal bindingi549 – 5491Magnesium; via carbonyl oxygen By similarity
Metal bindingi551 – 5511Magnesium; via carbonyl oxygen By similarity
Metal bindingi554 – 5541Magnesium; via carbonyl oxygen By similarity
Binding sitei596 – 5961Coenzyme A

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

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 synthetase (EC:6.2.1.1)
Short name:
AcCoA synthetase
Short name:
Acs
Alternative name(s):
Acetate--CoA ligase
Acyl-activating enzyme
Gene namesi
Name:acsA
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 synthetaseUniRule annotation
PRO_0000208360Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei621 – 6211N6-acetyllysine By similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation

Interactioni

Protein-protein interaction databases

STRINGi194439.CT1652.

Structurei

3D structure databases

ProteinModelPortaliQ8KBY0.
SMRiQ8KBY0. Positions 23-656.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni423 – 4286Substrate binding By similarity

Sequence similaritiesi

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

MATEQTKGQS SESISSVLSE RRKFPPPEAF SSQSHISSME QYEKLYADAA    50
ADPDKYWGDL AEQFHWFKKW DSVLEWNAPY AKWFNGGTTN IAYNCLDVHV 100
GSWRKNKAAI IWEGEEGNER ILTYGELHRQ VSKFANVLKI AGIKPGDKVA 150
IYMGMVPELV IAVLACARVG AVHNVIFAGF AAHAITERVN DSRAKIVICA 200
DGTRRRGSTI NLKNIVDEAI INTPSVKNVI VLKVTGEEIH MHDGMDHWWH 250
DLMGLAVDEC EPAQVDSEHP LFLLYTSGST GKPKGILHTT AGYMVHAASS 300
FKYVFDIKDE DIYFCTADIG WITGHTYIIY GPLLNGATVF MYEGAPNYPQ 350
WDRFWDIINR HKITILYTAP TAIRAFIRAG NEWVTKHDLS SLRLLGTVGE 400
PINPEAWMWY HKYVGQEKCP IVDTWWQTET GGIMISPMPG ATPTKPGTAT 450
RPLPGIMVDV VRKDGTPCNA NEGGYLVVKR PWPSMLRTIY GDNERYEKTY 500
WSEFPGMYFT GDGARKDDDG YIWIMGRVDD VVNVSGHRLG TSEVESALVS 550
HEAVAEAAVV SRPDEIKGNA LVAFVTLKDG YEGDAKLRDS LGKHVAKEIG 600
AIAKPDEIRW AKGLPKTRSG KIMRRLLREL ATSNEIKGDV TTLEDLGVIE 650
NLREQEDEG 659
Length:659
Mass (Da):73,576
Last modified:September 26, 2003 - v2
Checksum:i2BB84C9AB13EA034
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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: May 14, 2014
This is version 70 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

Similar proteinsi