Methylmalonyl-CoA carboxyltransferase 12S subunit - Propionibacterium freudenreichii subsp. shermanii

Contribute

Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q8GBW6 (12S_PROFR)

Last modified November 24, 2009. Version 45. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein names	Recommended name: Methylmalonyl-CoA carboxyltransferase 12S subunit EC=2.1.3.1 Alternative name(s): Transcarboxylase 12S subunit
Organism	Propionibacterium freudenreichii subsp. shermanii
Taxonomic identifier	1752 [NCBI]
Taxonomic lineage	Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Propionibacterineae › Propionibacteriaceae › Propionibacterium

Protein attributes

Sequence length	611 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	The 12S subunit specifically catalyzes the transfer of the carboxyl group of methylmalonyl CoA to the biotin of the 1.3S subunit forming propanoyl-CoA and carboxylated 1.3S-biotin.
Catalytic activity	(S)-methylmalonyl-CoA + pyruvate = propanoyl-CoA + oxaloacetate.
Subunit structure	Homohexamer. 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).
Sequence similarities	Contains 1 carboxyltransferase domain.
Sequence caution	The sequence AAA25676.1 differs from that shown. Reason: Frameshift at several positions. The sequence CAD59919.1 differs from that shown. Reason: Frameshift at position 519.

Ontologies

Keywords
Molecular function	Transferase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	acetyl-CoA carboxylase complex Inferred from electronic annotation. Source: InterPro
Molecular function	acetyl-CoA carboxylase activity Inferred from electronic annotation. Source: InterPro methylmalonyl-CoA carboxytransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

Removed Ref.1

Chain

610

Methylmalonyl-CoA carboxyltransferase 12S subunit

PRO_0000146817

Experimental info

Sequence conflict

1

R → L in AAA25676. Ref.1

Sequence conflict

1

Missing in AAA25676. Ref.1

Sequence conflict

2

GG → C in AAA25676. Ref.1

Sequence conflict

1

Missing in AAA25676. Ref.1

Sequence conflict

1

A → R in AAA25676. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

611

Helix Strand Turn

Sequences

Sequence

Length

Mass (Da)

Tools

Q8GBW6-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 625F1B284107B1FC
Show »

611

65,927

        10         20         30         40         50         60 
MAENNNLKLA STMEGRVEQL AEQRQVIEAG GGERRVEKQH SQGKQTARER LNNLLDPHSF 

        70         80         90        100        110        120 
DEVGAFRKHR TTLFGMDKAV VPADGVVTGR GTILGRPVHA ASQDFTVMGG SAGETQSTKV 

       130        140        150        160        170        180 
VETMEQALLT GTPFLFFYDS GGARIQEGID SLSGYGKMFF ANVKLSGVVP QIAIIAGPCA 

       190        200        210        220        230        240 
GGASYSPALT DFIIMTKKAH MFITGPQVIK SVTGEDVTAD ELGGAEAHMA ISGNIHFVAE 

       250        260        270        280        290        300 
DDDAAELIAK KLLSFLPQNN TEEASFVNPN NDVSPNTELR DIVPIDGKKG YDVRDVIAKI 

       310        320        330        340        350        360 
VDWGDYLEVK AGYATNLVTA FARVNGRSVG IVANQPSVMS GCLDINASDK AAEFVNFCDS 

       370        380        390        400        410        420 
FNIPLVQLVD VPGFLPGVQQ EYGGIIRHGA KMLYAYSEAT VPKITVVLRK AYGGSYLAMC 

       430        440        450        460        470        480 
NRDLGADAVY AWPSAEIAVM GAEGAANVIF RKEIKAADDP DAMRAEKIEE YQNAFNTPYV 

       490        500        510        520        530        540 
AAARGQVDDV IDPADTRRKI ASALEMYATK RQTRPAKKPW KLPLLSEEEI MADEEEKDLM 

       550        560        570        580        590        600 
IATLNKRVAS LESELGSLQS DTQGVTEDVL TAISAVAAYL GNDGSAEVVH FAPSPNWVRE 

       610 
GRRALQNHSI R

References

[1]

"Primary structure of the monomer of the 12S subunit of transcarboxylase as deduced from DNA and characterization of the product expressed in Escherichia coli."
Thornton C.G., Kumar G.K., Haase F.C., Phillips N.F.B., Woo S.B., Park V.M., Magner W.J., Shenoy B.C., Wood H.G., Samols D.
J. Bacteriol. 175:5301-5308(1993) [PubMed: 8366018] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-6; 13-39; 56-63; 71-112; 199-213; 252-280; 351-372; 395-405; 500-516; 532-567 AND 598-607.
Strain: St33.

[2]

"Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core."
Hall P.R., Wang Y.-F., Rivera-Hainaj R.E., Zheng X., Pusztai-Carey M., Carey P.R., Yee V.C.
EMBO J. 22:2334-2347(2003) [PubMed: 12743028] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-525, X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-524.

Cross-references

Sequence databases

L04196 Genomic DNA. Translation: AAA25676.1. Frameshift.
AJ535715 mRNA. Translation: CAD59919.1. Frameshift.

PIR

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ON3	X-ray	1.90	A/B/C/D/E/F	2-518	[»]
1ON9	X-ray	2.00	A/B/C/D/E/F	2-518	[»]

ModBase

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-12429.

BRENDA

2.1.3.1. 4086.

Family and domain databases

InterPro

IPR000438. Acetyl_CoA_COase_Trfase_b_su.
IPR000022. Carboxyl_trans.
IPR011763. COA_CT_C.
IPR011762. COA_CT_N.
[Graphical view]

Pfam

PF01039. Carboxyl_trans. 1 hit.
[Graphical view]

PRINTS

PR01070. ACCCTRFRASEB.

PROSITE

PS50989. COA_CT_CTER. 1 hit.
PS50980. COA_CT_NTER. 1 hit.
[Graphical view]

ProtoNet

Entry information

Entry name

12S_PROFR

Accession

Primary (citable) accession number: Q8GBW6
Secondary accession number(s): Q05617

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2005
Last sequence update:	January 23, 2007
Last modified:	November 24, 2009
This is version 45 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents