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Q70AC7 (5S_PROFR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methylmalonyl-CoA carboxyltransferase 5S subunit

EC=2.1.3.1
Alternative name(s):
Transcarboxylase 5S subunit
OrganismPropionibacterium freudenreichii subsp. shermanii
Taxonomic identifier1752 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesPropionibacterineaePropionibacteriaceaePropionibacterium

Protein attributes

Sequence length505 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The 5S subunit specifically catalyzes the transfer of the carboxyl group from biotin of the 1.3S subunit to pyruvate to form oxaloacetate and 1.3S biotin.

Catalytic activity

(S)-methylmalonyl-CoA + pyruvate = propanoyl-CoA + oxaloacetate.

Cofactor

Binds 1 Co2+ ion per subunit.

Subunit structure

Homodimer. Transcarboxylase is composed of three subunits: 1.3S, 5S, and 12S. The core of the enzyme is composed of six 12S subunits. On each side of the core there are three pairs of 5S subunits. Each 5S dimer is attached to the core by two 1.3S subunits. Thus the total number of chains is 30 (6 + 12 + 12). Ref.3

Post-translational modification

Lys-184 is carbamylated in the free enzyme and helps to coordinate the cobalt ion. Lys-184 is partially carbamylated in the complex with pyruvate, but is not carbamylated in the oxaloacetate-bound form.

Sequence similarities

Contains 1 carboxyltransferase domain.

Sequence caution

The sequence AAA03174.1 differs from that shown. Reason: Frameshift at positions 205, 217, 340, 344, 360, 426, 428, 457, 460, 463, 474, 480, 494 and 499.

Ontologies

Keywords
   LigandCobalt
Metal-binding
   Molecular functionTransferase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

methylmalonyl-CoA carboxytransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 505505Methylmalonyl-CoA carboxyltransferase 5S subunit
PRO_0000146816

Regions

Region22 – 265Substrate binding

Sites

Metal binding231Cobalt
Metal binding1841Cobalt
Metal binding2151Cobalt
Metal binding2171Cobalt
Binding site591Substrate; via amide nitrogen
Binding site1841Substrate

Amino acid modifications

Modified residue1841N6-carboxylysine; partial

Experimental info

Mutagenesis591A → T: Decreases activity by 96%. Ref.3
Mutagenesis1841K → A or E: Loss of activity. Ref.3
Mutagenesis1861M → I: Decreases activity by 98%. Ref.3
Sequence conflict3411A → AG in AAA03174. Ref.1
Sequence conflict3861S → T in AAA03174. Ref.1
Sequence conflict3901R → RDPKWSVGEEHRRAITQRPA DH in AAA03174. Ref.1
Sequence conflict4211K → E in AAA03174. Ref.1
Sequence conflict4291L → P in AAA03174. Ref.1
Sequence conflict4551H → S in AAA03174. Ref.1
Sequence conflict4611H → Q in AAA03174. Ref.1
Sequence conflict4811L → V in AAA03174. Ref.1

Secondary structure

.................................................................................... 505
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q70AC7 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 6DF657E231609064

FASTA50555,649
        10         20         30         40         50         60 
MSPREIEVSE PREVGITELV LRDAHQSLMA TRMAMEDMVG ACADIDAAGY WSVECWGGAT 

        70         80         90        100        110        120 
YDSCIRFLNE DPWERLRTFR KLMPNSRLQM LLRGQNLLGY RHYNDEVVDR FVDKSAENGM 

       130        140        150        160        170        180 
DVFRVFDAMN DPRNMAHAMA AVKKAGKHAQ GTICYTISPV HTVEGYVKLA GQLLDMGADS 

       190        200        210        220        230        240 
IALKDMAALL KPQPAYDIIK AIKDTYGQKT QINLHCHSTT GVTEVSLMKA IEAGVDVVDT 

       250        260        270        280        290        300 
AISSMSLGPG HNPTESVAEM LEGTGYTTNL DYDRLHKIRD HFKAIRPKYK KFESKTLVDT 

       310        320        330        340        350        360 
SIFKSQIPGG MLSNMESQLR AQGAEDKMDE VMAEVPRVRK AAGFPPLVTP SSQIVGTQAV 

       370        380        390        400        410        420 
FNVMMGEYKR MTGEFADIML GYYGASPADR DPKVVKLAEE QSGKKPITQR PADLLPPEWE 

       430        440        450        460        470        480 
KQSKEAATLK GFNGTDEDVL TYALFPQVAP VFFEHRAEGP HSVALTDAQL KAEAEGDEKS 

       490        500 
LAVAGPVTYN VNVGGTVREV TVQQA 

« Hide

References

[1]"Primary structure of the 5 S subunit of transcarboxylase as deduced from the genomic DNA sequence."
Thornton C.G., Kumar G.K., Shenoy B.C., Haase F.C., Phillips N.F.B., Park V.M., Magner W.J., Hejlik D.P., Wood H.G., Samols D.
FEBS Lett. 330:191-196(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 3-22; 67-76; 88-92; 111-124; 134-147; 305-316; 325-337; 371-393; 397-410 AND 431-456.
Strain: St33.
[2]"Expression and crystallization of several forms of the Propionibacterium shermanii transcarboxylase 5S subunit."
Hall P.R., Zheng R., Pusztai-Carey M., van den Akker F., Carey P.R., Yee V.C.
Acta Crystallogr. D 60:521-523(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 13673 / VPI 0409 / 33.
[3]"Transcarboxylase 5S structures: assembly and catalytic mechanism of a multienzyme complex subunit."
Hall P.R., Zheng R., Antony L., Pusztai-Carey M., Carey P.R., Yee V.C.
EMBO J. 23:3621-3631(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEXES WITH SUBSTRATE; PRODUCT AND COBALT IONS, SUBUNIT, CARBAMYLATION AT LYS-184, MUTAGENESIS OF ALA-59; LYS-184 AND MET-186.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L06488 Unassigned DNA. Translation: AAA03174.1. Frameshift.
AJ606310 Genomic DNA. Translation: CAE54442.1.
PIRS36808.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1RQBX-ray1.90A2-505[»]
1RQEX-ray2.50A2-505[»]
1RQHX-ray2.00A2-505[»]
1RR2X-ray2.00A2-505[»]
1S3HX-ray2.50A2-505[»]
1U5JX-ray2.80A2-505[»]
ProteinModelPortalQ70AC7.
SMRQ70AC7. Positions 3-474.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-12430.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR003379. Carboxylase_cons_dom.
IPR000891. PYR_CT.
[Graphical view]
PfamPF00682. HMGL-like. 1 hit.
PF02436. PYC_OADA. 1 hit.
[Graphical view]
PROSITEPS50991. PYR_CT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ70AC7.

Entry information

Entry name5S_PROFR
AccessionPrimary (citable) accession number: Q70AC7
Secondary accession number(s): Q05618
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references