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Protein

Succinyl-CoA:acetate CoA-transferase

Gene
N/A
Organism
Acetobacter aceti
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Utilizes succinyl-CoA to convert toxic acetate to acetyl-CoA and succinate. Required for growth on acetic acid and for resistance to high levels of acetic acid. Has also low activity with acetoacetate as substrate.4 Publications

Catalytic activityi

Succinyl-CoA + acetate = acetyl-CoA + succinate.3 Publications

Enzyme regulationi

Subject to competitive inhibition by coenzyme A (CoA).1 Publication

Kineticsi

kcat is 280 s(-1) with acetate. kcat is 201 s(-1) with succinyl-CoA. kcat is 75 s(-1) with acetyl-CoA. kcat is 36.5 s(-1) with acetoacetate. kcat is 70.9 s(-1) with succinate.1 Publication

  1. KM=70 mM for acetate.1 Publication
  2. KM=22.1 mM for succinyl-CoA.1 Publication
  3. KM=22.3 mM for acetyl-CoA.1 Publication
  4. KM=0.9 mM for succinate.1 Publication
  5. KM=130 mM for acetoacetate.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei294 – 29415-glutamyl coenzyme A thioester intermediate1 Publication
Binding sitei364 – 3641Coenzyme A; via carbonyl oxygen1 Publication
Binding sitei384 – 3841Coenzyme A1 Publication
Binding sitei388 – 3881Coenzyme A; via amide nitrogen1 Publication
Binding sitei408 – 4081Coenzyme A1 Publication

GO - Molecular functioni

  1. transferase activity Source: UniProtKB

GO - Biological processi

  1. acetate catabolic process Source: UniProtKB
  2. acetyl-CoA biosynthetic process from acetate Source: UniProtKB
  3. succinyl-CoA catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17982.
UniPathwayiUPA00340.

Names & Taxonomyi

Protein namesi
Recommended name:
Succinyl-CoA:acetate CoA-transferase (EC:2.8.3.183 Publications)
Alternative name(s):
Succinyl-coenzyme A (CoA):acetate CoA-transferase2 Publications
Short name:
SCACT1 Publication
OrganismiAcetobacter acetiImported
Taxonomic identifieri435 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeAcetobacterAcetobacter subgen. Acetobacter

Pathology & Biotechi

Disruption phenotypei

Cells cannot grow on acetate and have lost the resistance to high levels of acetate, a characteristic of wild-type A.aceti.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi294 – 2941E → A: Abolishes enzyme activity. 1 Publication
Mutagenesisi357 – 3571C → Y: Strongly impaired protein solubility. 1 Publication
Mutagenesisi435 – 4351E → A or Q: Abolishes protein solubility. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 505505Succinyl-CoA:acetate CoA-transferasePRO_0000430783Add
BLAST

Expressioni

Inductioni

Expressed at intermediate levels during the first growth phase, when ethanol is metabolized and acetic acid accumulates in the growth medium. Up-regulated during the second growth phase, when acetate is catabolized.1 Publication

Interactioni

Subunit structurei

Homodimer.2 Publications

Structurei

Secondary structure

1
505
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 135Combined sources
Helixi17 – 215Combined sources
Beta strandi29 – 324Combined sources
Helixi43 – 5715Combined sources
Beta strandi64 – 674Combined sources
Turni74 – 763Combined sources
Helixi77 – 826Combined sources
Beta strandi86 – 916Combined sources
Helixi96 – 1038Combined sources
Beta strandi106 – 1094Combined sources
Helixi114 – 1163Combined sources
Helixi117 – 1237Combined sources
Turni124 – 1263Combined sources
Beta strandi131 – 1399Combined sources
Beta strandi145 – 1473Combined sources
Helixi154 – 1607Combined sources
Beta strandi162 – 1698Combined sources
Helixi174 – 1763Combined sources
Beta strandi179 – 1824Combined sources
Beta strandi187 – 1926Combined sources
Beta strandi206 – 2105Combined sources
Helixi214 – 2163Combined sources
Beta strandi217 – 2237Combined sources
Helixi237 – 25519Combined sources
Beta strandi266 – 2683Combined sources
Helixi272 – 28312Combined sources
Beta strandi288 – 2969Combined sources
Helixi298 – 3069Combined sources
Beta strandi307 – 31711Combined sources
Helixi321 – 3299Combined sources
Helixi331 – 3355Combined sources
Beta strandi338 – 3425Combined sources
Helixi343 – 3464Combined sources
Helixi349 – 3557Combined sources
Beta strandi358 – 3614Combined sources
Beta strandi364 – 3674Combined sources
Beta strandi372 – 3776Combined sources
Turni378 – 3803Combined sources
Helixi389 – 3957Combined sources
Beta strandi396 – 4027Combined sources
Beta strandi405 – 4073Combined sources
Turni408 – 4114Combined sources
Beta strandi412 – 4187Combined sources
Helixi426 – 4283Combined sources
Beta strandi431 – 4344Combined sources
Beta strandi437 – 4404Combined sources
Helixi446 – 45611Combined sources
Turni460 – 4623Combined sources
Helixi463 – 47614Combined sources
Beta strandi478 – 4825Combined sources
Turni486 – 4905Combined sources
Helixi491 – 4999Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4EU3X-ray1.58A/B1-505[»]
4EU4X-ray2.80A/B1-505[»]
4EU5X-ray1.74A/B1-505[»]
4EU6X-ray1.99A/B1-505[»]
4EU7X-ray1.70A/B1-505[»]
4EU8X-ray1.81A/B1-505[»]
4EU9X-ray1.48A/B1-505[»]
4EUAX-ray2.40A/B1-505[»]
4EUBX-ray1.97A/B1-505[»]
4EUCX-ray2.64A/B1-505[»]
4EUDX-ray1.95A/B1-505[»]
4FACX-ray2.05A/B1-505[»]
ProteinModelPortaliB3EY95.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni269 – 2735Coenzyme A binding1 Publication

Sequence similaritiesi

Family and domain databases

InterProiIPR026888. AcetylCoA_hyd_C.
IPR003702. ActCoA_hydro.
IPR017821. Succinate_CoA_transferase.
[Graphical view]
PfamiPF13336. AcetylCoA_hyd_C. 1 hit.
PF02550. AcetylCoA_hydro. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03458. YgfH_subfam. 1 hit.

Sequencei

Sequence statusi: Complete.

B3EY95-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTERIRNVAL RSKVCPAETA SELIKHGDVV GTSGFTGAGY PKEVPKALAQ
60 70 80 90 100
RMEAAHDRGE KYQISLITGA STGPQLDGEL AKANGVYFRS PFNTDATMRN
110 120 130 140 150
RINAGETEYF DNHLGQVAGR AVQGNYGKFN IALVEATAIT EDGGIVPTSS
160 170 180 190 200
VGNSQTFLNL AEKVIIEVNE WQNPMLEGIH DIWDGNVSGV PTRDIVPIVR
210 220 230 240 250
ADQRVGGPVL RVNPDKIAAI VRTNDRDRNA PFAAPDETAK AIAGYLLDFF
260 270 280 290 300
GHEVKQNRLP PSLLPLQSGV GNVANAVLEG LKEGPFENLV GYSEVIQDGM
310 320 330 340 350
LAMLDSGRMR IASASSFSLS PEAAEEINNR MDFFRSKIIL RQQDVSNSPG
360 370 380 390 400
IIRRLGCIAM NGMIEADIYG NVNSTRVMGS KMMNGIGGSG DFARSSYLSI
410 420 430 440 450
FLSPSTAKGG KISAIVPMAA HVDHIMQDAQ IFVTEQGLAD LRGLSPVQRA
460 470 480 490 500
REIISKCAHP DYRPMLQDYF DRALKNSFGK HTPHLLTEAL SWHQRFIDTG

TMLPS
Length:505
Mass (Da):54,826
Last modified:July 22, 2008 - v1
Checksum:iC02A8779588D2510
GO

Sequence cautioni

The sequence BAA02549.1 differs from that shown. Reason: Frameshift at position 54. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti357 – 3571C → Y in AGG68324. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13291 Genomic DNA. Translation: BAA02549.1. Frameshift.
DQ631551 Genomic DNA. Translation: ACD85596.1.
JX475924 Genomic DNA. Translation: AGG68319.1.
JX475925 Genomic DNA. Translation: AGG68324.1.
PIRiI39486.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13291 Genomic DNA. Translation: BAA02549.1. Frameshift.
DQ631551 Genomic DNA. Translation: ACD85596.1.
JX475924 Genomic DNA. Translation: AGG68319.1.
JX475925 Genomic DNA. Translation: AGG68324.1.
PIRiI39486.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4EU3X-ray1.58A/B1-505[»]
4EU4X-ray2.80A/B1-505[»]
4EU5X-ray1.74A/B1-505[»]
4EU6X-ray1.99A/B1-505[»]
4EU7X-ray1.70A/B1-505[»]
4EU8X-ray1.81A/B1-505[»]
4EU9X-ray1.48A/B1-505[»]
4EUAX-ray2.40A/B1-505[»]
4EUBX-ray1.97A/B1-505[»]
4EUCX-ray2.64A/B1-505[»]
4EUDX-ray1.95A/B1-505[»]
4FACX-ray2.05A/B1-505[»]
ProteinModelPortaliB3EY95.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00340.
BioCyciMetaCyc:MONOMER-17982.

Family and domain databases

InterProiIPR026888. AcetylCoA_hyd_C.
IPR003702. ActCoA_hydro.
IPR017821. Succinate_CoA_transferase.
[Graphical view]
PfamiPF13336. AcetylCoA_hyd_C. 1 hit.
PF02550. AcetylCoA_hydro. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03458. YgfH_subfam. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The aarC gene responsible for acetic acid assimilation confers acetic acid resistance on Acetobacter aceti."
    Fukaya M., Takemura H., Tayama K., Okumura H., Kawamura Y., Horinouchi S., Beppu T.
    J. Ferment. Bioeng. 76:270-275(1993)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, DISRUPTION PHENOTYPE, FUNCTION.
    Strain: 1023Imported.
  2. "A specialized citric acid cycle requiring succinyl-coenzyme A (CoA):acetate CoA-transferase (AarC) confers acetic acid resistance on the acidophile Acetobacter aceti."
    Mullins E.A., Francois J.A., Kappock T.J.
    J. Bacteriol. 190:4933-4940(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, PATHWAY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: 10231 Publication.
  3. "Functional analysis of the acetic acid resistance (aar) gene cluster in Acetobacter aceti strain 1023."
    Mullins E.A., Kappock T.J.
    Acetic Acid Bacteria 2:E3-E3(2013)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-357, PATHWAY, INDUCTION.
    Strain: 10231 Publication.
  4. "Crystal structures of Acetobacter aceti succinyl-coenzyme A (CoA):acetate CoA-transferase reveal specificity determinants and illustrate the mechanism used by class I CoA-transferases."
    Mullins E.A., Kappock T.J.
    Biochemistry 51:8422-8434(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) IN COMPLEXES WITH COENZYME A AND ACETATE, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, MUTAGENESIS OF GLU-435.

Entry informationi

Entry nameiSCACT_ACEAC
AccessioniPrimary (citable) accession number: B3EY95
Secondary accession number(s): M4MDU8, Q43882
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 29, 2014
Last sequence update: July 22, 2008
Last modified: January 7, 2015
This is version 22 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.