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C1DFK2

- C1DFK2_AZOVD

UniProt

C1DFK2 - C1DFK2_AZOVD

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Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Azotobacter vinelandii (strain DJ / ATCC BAA-1303)
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 annotationSAAS annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei308 – 3081Coenzyme AUniRule annotation
Binding sitei332 – 3321Coenzyme AUniRule annotation
Binding sitei497 – 4971ATPUniRule annotation
Binding sitei512 – 5121ATPUniRule annotation
Binding sitei520 – 5201Coenzyme A; via carbonyl oxygenUniRule annotation
Binding sitei523 – 5231ATPUniRule annotation
Metal bindingi534 – 5341Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi536 – 5361Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi539 – 5391Magnesium; via carbonyl oxygenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi384 – 3863ATPUniRule annotation
Nucleotide bindingi408 – 4136ATPUniRule 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 annotationImported

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciAVIN322710:GJ0M-4277-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:acsA2Imported
Ordered Locus Names:Avin_42750Imported
OrganismiAzotobacter vinelandii (strain DJ / ATCC BAA-1303)Imported
Taxonomic identifieri322710 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeAzotobacter
ProteomesiUP000002424: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei606 – 6061N6-acetyllysineUniRule annotation

Post-translational modificationi

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

Keywords - PTMi

AcetylationUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi322710.Avin_42750.

Structurei

3D structure databases

ProteinModelPortaliC1DFK2.
SMRiC1DFK2. Positions 7-642.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni190 – 1934Coenzyme A bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0365.
HOGENOMiHOG000229981.
KOiK01895.
OMAiKSLENPE.
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.

C1DFK2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFKIANHPVS EALRQHSWLN NDDYLRLYRQ SVEQPDSFWA EQATLFLDWF
60 70 80 90 100
KPWRNIHRGD MNKGEIHWFE GSQLNVAHNC IDRHLKQRGD QVAIIWEGDN
110 120 130 140 150
PADSARITYR QLHEQVCRLA NLLKSRGIGK GDRVCIYMPM IPEAAYAMLA
160 170 180 190 200
CARIGAVHSV VFGGFSPEAL RDRILDADCR LLITADESVR GGKVVPLKRN
210 220 230 240 250
ADKALQSCSG VSSVIVVRRT GGAIDWNVGR DLWYHEAVPG CSADCPAEPM
260 270 280 290 300
DAEAPLFILY TSGSTGKPKG VLHTTGGYLL QAAMTHQYVF DYHDGDIYWC
310 320 330 340 350
SADIGWITGH SYIVYGPLAN GATTLIFEGV PNYPDASRFW QVVDKHRVNI
360 370 380 390 400
FYTAPTALRS LMREGEGPVR KTSRASLRLL GSVGEPINPE AWEWYYHVVG
410 420 430 440 450
DSRCPIVDTW WQTETGAIMI TPLPGATLLK PGSATRPFFG VQPVLLDDKG
460 470 480 490 500
KEIEGPGAGI LAIKASWPSQ IRSIYGDHQR LIDTYFKPCP GYYFTGDGAR
510 520 530 540 550
RDEDGYYWIT GRVDDVINVS GHRIGTAEVE SALVLHDSIA EAAVVGCPHD
560 570 580 590 600
VKGQCVYAFV TLVTGSRPSD QLKRELIDQV SREIGGFAKP DFLQWAPRLP
610 620 630 640
KTRSGKIMRR ILRKIACNEL DNLGDTSTLS DPSVLQELID NRLSH
Length:645
Mass (Da):71,897
Last modified:May 26, 2009 - v1
Checksum:i2196F80A1AE5C342
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001157 Genomic DNA. Translation: ACO80398.1.
RefSeqiYP_002801373.1. NC_012560.1.

Genome annotation databases

EnsemblBacteriaiACO80398; ACO80398; Avin_42750.
GeneIDi7763150.
KEGGiavn:Avin_42750.
PATRICi21034580. VBIAzoVin72790_4023.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001157 Genomic DNA. Translation: ACO80398.1 .
RefSeqi YP_002801373.1. NC_012560.1.

3D structure databases

ProteinModelPortali C1DFK2.
SMRi C1DFK2. Positions 7-642.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 322710.Avin_42750.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACO80398 ; ACO80398 ; Avin_42750 .
GeneIDi 7763150.
KEGGi avn:Avin_42750.
PATRICi 21034580. VBIAzoVin72790_4023.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci AVIN322710:GJ0M-4277-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: DJ / ATCC BAA-1303Imported.

Entry informationi

Entry nameiC1DFK2_AZOVD
AccessioniPrimary (citable) accession number: C1DFK2
Entry historyi
Integrated into UniProtKB/TrEMBL: May 26, 2009
Last sequence update: May 26, 2009
Last modified: November 26, 2014
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3