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Q30QK3 (Q30QK3_SULDN) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein attributes

Sequence length651 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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. HAMAP-Rule MF_01123

Catalytic activity

ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA. HAMAP-Rule MF_01123

Cofactor

Magnesium By similarity. HAMAP-Rule MF_01123 SAAS SAAS011904

Post-translational modification

Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme By similarity. HAMAP-Rule MF_01123

Sequence similarities

Belongs to the ATP-dependent AMP-binding enzyme family. HAMAP-Rule MF_01123

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site5171 By similarity HAMAP-Rule MF_01123
Metal binding5391Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5421Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Binding site3071Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3831Substrate; via nitrogen amide By similarity HAMAP-Rule MF_01123
Binding site5001Substrate By similarity HAMAP-Rule MF_01123
Binding site5151Substrate By similarity HAMAP-Rule MF_01123
Binding site5231Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site5261Substrate By similarity HAMAP-Rule MF_01123
Binding site5861Coenzyme A By similarity HAMAP-Rule MF_01123

Amino acid modifications

Modified residue6111N6-acetyllysine By similarity HAMAP-Rule MF_01123

Sequences

Sequence LengthMass (Da)Tools
Q30QK3 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: 7A53E3EDCBB4CCC8

FASTA65172,616
        10         20         30         40         50         60 
MNREVFKPNK EFSKSARIKN MCEYQDLQEY ALEDYEGFWG SYAKEKLEWM QPFTNVMNES 

        70         80         90        100        110        120 
NFPFVKWFEG GKLNVSVQCI DRHLKSRKNK AAIIFEGDRG DKQIITYLEL YYNVNKFANL 

       130        140        150        160        170        180 
LKNEFDVKKG DRVIIYMPMI PEAAYAMLAC ARIGAIHSIV FGGFSAEALK DRVIDAGAKV 

       190        200        210        220        230        240 
VITADGAYRK DKPYMLKPVV DEALRGETPV KKVLVVERNG EDVTWVAGRD YSYNELIKHQ 

       250        260        270        280        290        300 
SGKCEPEVMD SEDPLFLLYT SGSTGKPKGV QHNSAGYILW AQMTMEWVFD VKENDTYWCT 

       310        320        330        340        350        360 
ADVGWITGHT YIVYGPLAMG ATTIMFEGVP TYPDAGRPWK MVEEYKVNQF YTAPTAIRVL 

       370        380        390        400        410        420 
HKTGENEPAK YDLSSLKVLG TVGEPIDPPA WKWYYEAIGG SKCAIVDTYW QTETGGHIVS 

       430        440        450        460        470        480 
PLPGATPIKP ACATFPLPGI MAEILDENGN RAEVGEKGLM CVTRPWPAMI RGVWGDEERF 

       490        500        510        520        530        540 
VKSYFGDVKK DGKPVYFTGD GAIYDEDGYI TITGRTDDVI NVSGHRMGTA EVEAAIKKHP 

       550        560        570        580        590        600 
NVAEVAVVGK PHEIKGEGIF AYIVLKSDSG IADEVEEVKA INKVIQKEIG NIALCDDVVF 

       610        620        630        640        650 
VVGLPKTRSG KIMRRILRSI AKGEEITQDI STLEDPSIVA TIASAVQSCR L 

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References

[1]"Genome of the epsilonproteobacterial chemolithoautotroph Sulfurimonas denitrificans."
Sievert S.M., Scott K.M., Klotz M.G., Chain P.S., Hauser L.J., Hemp J., Hugler M., Land M., Lapidus A., Larimer F.W., Lucas S., Malfatti S.A., Meyer F., Paulsen I.T., Ren Q., Simon J., USF Genomics Class
Appl. Environ. Microbiol. 74:1145-1156(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33889 / DSM 1251.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000153 Genomic DNA. Translation: ABB44728.1.
RefSeqYP_393963.1. NC_007575.1.

3D structure databases

ProteinModelPortalQ30QK3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING326298.Suden_1451.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB44728; ABB44728; Suden_1451.
GeneID3763349.
KEGGtdn:Suden_1451.
PATRIC23771544. VBISulDen68967_1506.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHOG000229981.
KOK01895.
OMAGGCEAVT.
OrthoDBEOG68WR2H.

Enzyme and pathway databases

BioCycSDEN326298:GH9P-1500-MONOMER.

Family and domain databases

HAMAPMF_01123. Ac_CoA_synth.
InterProIPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
TIGRFAMsTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ30QK3_SULDN
AccessionPrimary (citable) accession number: Q30QK3
Entry history
Integrated into UniProtKB/TrEMBL: December 6, 2005
Last sequence update: December 6, 2005
Last modified: June 11, 2014
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)