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B3EY95

- SCACT_ACEAC

UniProt

B3EY95 - SCACT_ACEAC

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Protein

Succinyl-CoA:acetate CoA-transferase

Gene
N/A
Organism
Acetobacter aceti
Status
Reviewed - 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-KW

GO - Biological processi

  1. acetyl-CoA metabolic process Source: InterPro
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

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 .
PIRi I39486.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4EU3 X-ray 1.58 A/B 1-505 [» ]
4EU4 X-ray 2.80 A/B 1-505 [» ]
4EU5 X-ray 1.74 A/B 1-505 [» ]
4EU6 X-ray 1.99 A/B 1-505 [» ]
4EU7 X-ray 1.70 A/B 1-505 [» ]
4EU8 X-ray 1.81 A/B 1-505 [» ]
4EU9 X-ray 1.48 A/B 1-505 [» ]
4EUA X-ray 2.40 A/B 1-505 [» ]
4EUB X-ray 1.97 A/B 1-505 [» ]
4EUC X-ray 2.64 A/B 1-505 [» ]
4EUD X-ray 1.95 A/B 1-505 [» ]
4FAC X-ray 2.05 A/B 1-505 [» ]
ProteinModelPortali B3EY95.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00340 .
BioCyci MetaCyc:MONOMER-17982.

Family and domain databases

InterProi IPR026888. AcetylCoA_hyd_C.
IPR003702. ActCoA_hydro.
IPR017821. Succinate_CoA_transferase.
[Graphical view ]
Pfami PF13336. AcetylCoA_hyd_C. 1 hit.
PF02550. AcetylCoA_hydro. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR03458. YgfH_subfam. 1 hit.
ProtoNeti Search...

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: October 29, 2014
This is version 21 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