Skip Header

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

Q47X57

- Q47X57_COLP3

UniProt

Q47X57 - Q47X57_COLP3

(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

acs

Organism
Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio psychroerythus)
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 sitei309 – 3091Coenzyme AUniRule annotation
Binding sitei498 – 4981ATPUniRule annotation
Binding sitei513 – 5131ATPUniRule annotation
Binding sitei521 – 5211Coenzyme A; via carbonyl oxygenUniRule annotation
Binding sitei524 – 5241ATPUniRule annotation
Metal bindingi535 – 5351Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi537 – 5371Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi540 – 5401Magnesium; via carbonyl oxygenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi385 – 3873ATPUniRule annotation
Nucleotide bindingi409 – 4146ATPUniRule 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

BioCyciCPSY167879:GI48-3955-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:acsImported
Synonyms:acsAUniRule annotation
Ordered Locus Names:CPS_3955Imported
OrganismiColwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio psychroerythus)Imported
Taxonomic identifieri167879 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesColwelliaceaeColwellia
ProteomesiUP000000547: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei607 – 6071N6-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

STRINGi167879.CPS_3955.

Structurei

3D structure databases

ProteinModelPortaliQ47X57.
SMRiQ47X57. Positions 20-643.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni191 – 1944Coenzyme A bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0365.
HOGENOMiHOG000229981.
KOiK01895.
OMAiHPPQKML.
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.

Q47X57-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKELKSCYPV SEKAKAHTHI DAATYDAMYK KSIEQPDEFW GEQAKEFIDW
60 70 80 90 100
YKPWDSVSKV DLKNSEINWF SGGKLNVSYN CIDRHLATKA NDTAIIFEGD
110 120 130 140 150
DPNDDSKVTY QELHDHVCRF ANLLKERGVK KGDRVCIYMP MIPEVGYAML
160 170 180 190 200
ACARIGAIHS VVFGGFSTES IKARVLDADC KVVITADQSL RGGKRIPLKS
210 220 230 240 250
NVDAAVIDCP NVHSVIVVAR TGGDVAWNDK VDINYEEAVA KQSAICEPEV
260 270 280 290 300
MDAEDPLFVL YTSGSTGTPK GVVHTCGGYI LYAAMTHKYV FDYKEGEVYW
310 320 330 340 350
CTADAGWITG HSYIFYGPLA NGATTLVFEG VPTYPDAGRF WQVCEKHKVN
360 370 380 390 400
VFYTAPTAIR ALMSIGDDLV NQADLSSLRL LGTVGEPINP EAWHWYYEVV
410 420 430 440 450
GKSNCPIVDT WWQTETGGIL ITSLPGAVDM KPGCAGKPFF GVQPALFDKD
460 470 480 490 500
GNTLEGENAG LLVMTASWPG QLRTVYGDHN RFYQTYLGQY PGNYFTGDGA
510 520 530 540 550
KRDEDGYYWI TGRVDDVLNV SGHRLGTAEI ESALVLHPAV AEAAVVGYPH
560 570 580 590 600
EIKGQGVYCY VTLMGNATES DELNVELREF VAKELGRFAK PDYIQWSPGL
610 620 630 640
PKTRSGKIMR RILRKIAEND VDSLGDTSTL ADPSVVENLI DKRIIHGA
Length:648
Mass (Da):71,614
Last modified:September 13, 2005 - v1
Checksum:i12B79CF080B776AB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000083 Genomic DNA. Translation: AAZ26507.1.
RefSeqiWP_011044699.1. NC_003910.7.
YP_270613.1. NC_003910.7.

Genome annotation databases

EnsemblBacteriaiAAZ26507; AAZ26507; CPS_3955.
GeneIDi3520759.
KEGGicps:CPS_3955.
PATRICi21470797. VBIColPsy94388_3583.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000083 Genomic DNA. Translation: AAZ26507.1 .
RefSeqi WP_011044699.1. NC_003910.7.
YP_270613.1. NC_003910.7.

3D structure databases

ProteinModelPortali Q47X57.
SMRi Q47X57. Positions 20-643.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 167879.CPS_3955.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAZ26507 ; AAZ26507 ; CPS_3955 .
GeneIDi 3520759.
KEGGi cps:CPS_3955.
PATRICi 21470797. VBIColPsy94388_3583.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci CPSY167879:GI48-3955-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: 34H / ATCC BAA-681Imported.

Entry informationi

Entry nameiQ47X57_COLP3
AccessioniPrimary (citable) accession number: Q47X57
Entry historyi
Integrated into UniProtKB/TrEMBL: September 13, 2005
Last sequence update: September 13, 2005
Last modified: November 26, 2014
This is version 59 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