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Protein

Acetyl-coenzyme A synthetase

Gene

Acss1

Organism
Rattus norvegicus (Rat)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

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

GO - Molecular functioni

  • acetate-CoA ligase activity Source: RGD
  • AMP binding Source: InterPro
  • ATP binding Source: UniProtKB-KW

GO - Biological processi

  • acetate biosynthetic process Source: RGD
  • acetyl-CoA biosynthetic process from acetate Source: InterPro
  • propionate biosynthetic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

LigaseUniRule annotation

Keywords - Ligandi

ATP-bindingUniRule annotation, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-RNO-71384. Ethanol oxidation.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-coenzyme A synthetaseUniRule annotation (EC:6.2.1.1UniRule annotation)
Gene namesi
Name:Acss1Imported
ORF Names:rCG_37494Imported
OrganismiRattus norvegicus (Rat)Imported
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 3

Organism-specific databases

RGDi1306246. Acss1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: Ensembl
  • mitochondrion Source: RGD
Complete GO annotation...

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000009627.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini51 – 10757ACAS_NInterPro annotationAdd
BLAST
Domaini109 – 548440AMP-bindingInterPro annotationAdd
BLAST
Domaini557 – 63579AMP-binding_CInterPro annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG1175. Eukaryota.
COG0365. LUCA.
GeneTreeiENSGT00760000119178.
KOiK01895.
OMAiAYRTEGG.
OrthoDBiEOG77T140.
TreeFamiTF354241.

Family and domain databases

InterProiIPR011904. Ac_CoA_lig.
IPR032387. ACAS_N.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF16177. ACAS_N. 1 hit.
PF00501. 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.

D3ZZN3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAARSLGSGV GRLLRGLHGH SGQSGWLLSL SRWTTTRFLG SVPAAAQLGS
60 70 80 90 100
YPALSAQAAQ EPAAFWGPLA RDTLVWDTPY HTVWDCDFRT GKIGWFLGGQ
110 120 130 140 150
LNVSVNCLDQ HVQKSPDTIA LIWERDEPGT EVRITYRELL ETTCRLANTL
160 170 180 190 200
KRHGVHRGDR VAIYMPVSPL AVAAMLACAR IGAIHTVVFA GFSAESLAGR
210 220 230 240 250
INDAKCKVVI TFNQGLRGGR VVELKKIVDE AVKNCPTVQH VLVAHRTDTK
260 270 280 290 300
VPMGNLDIPL EQEMANEAPV CTPESMNSED MLFMLYTSGS TGTPKGLVHT
310 320 330 340 350
QAGYLLYAAM THKLVFDYHP GDVFGCVADI GWITGHSYVV YGPLCNGATT
360 370 380 390 400
VLFESTPVYP DAGRYWETVQ RLKINQFYGA PTAVRLLLKF GDAWVKKYDR
410 420 430 440 450
SSLRTLGSVG EPINHEAWEW LHKVVGDGRC TLVDTWWQTE TGGICIAPRP
460 470 480 490 500
SEDGAEILPG MAMRPFFGIV PALMDEKGNV VEGGDVSGAL CISQAWPGMA
510 520 530 540 550
RTIYGDHQRF VDAYFRTYPG YYFTGDGAHR TEGGYYQITG RMDDVINISG
560 570 580 590 600
HRLGTAEIED AMADHPAVPE TAVIGYPHDI KGEAAFAFIV LKDDVRDANV
610 620 630 640 650
VVNELKLAVA TKIAKYAVPD QILVVKRLPK TRSGKVMRRL LRKIITSRGQ
660 670 680
DLGDTTTLED PSVITEIMSA FREYEEQRAA TN
Length:682
Mass (Da):74,892
Last modified:April 20, 2010 - v1
Checksum:iA9816B496C346055
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR07054290 Genomic DNA. No translation available.
CH474050 Genomic DNA. Translation: EDL86149.1.
RefSeqiNP_001099994.1. NM_001106524.1.
UniGeneiRn.98236.

Genome annotation databases

EnsembliENSRNOT00000009627; ENSRNOP00000009627; ENSRNOG00000007102.
GeneIDi296259.
KEGGirno:296259.
UCSCiRGD:1306246. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR07054290 Genomic DNA. No translation available.
CH474050 Genomic DNA. Translation: EDL86149.1.
RefSeqiNP_001099994.1. NM_001106524.1.
UniGeneiRn.98236.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000009627.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000009627; ENSRNOP00000009627; ENSRNOG00000007102.
GeneIDi296259.
KEGGirno:296259.
UCSCiRGD:1306246. rat.

Organism-specific databases

CTDi84532.
RGDi1306246. Acss1.

Phylogenomic databases

eggNOGiKOG1175. Eukaryota.
COG0365. LUCA.
GeneTreeiENSGT00760000119178.
KOiK01895.
OMAiAYRTEGG.
OrthoDBiEOG77T140.
TreeFamiTF354241.

Enzyme and pathway databases

ReactomeiR-RNO-71384. Ethanol oxidation.

Miscellaneous databases

NextBioi640872.

Family and domain databases

InterProiIPR011904. Ac_CoA_lig.
IPR032387. ACAS_N.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF16177. ACAS_N. 1 hit.
PF00501. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Rat Genome Sequencing Project Consortium
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown NorwayImported.
  2. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  3. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  4. Ensembl
    Submitted (JUL-2011) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Brown NorwayImported.

Entry informationi

Entry nameiD3ZZN3_RAT
AccessioniPrimary (citable) accession number: D3ZZN3
Entry historyi
Integrated into UniProtKB/TrEMBL: April 20, 2010
Last sequence update: April 20, 2010
Last modified: May 11, 2016
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.