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Protein

Methylmalonyl-CoA carboxyltransferase 12S subunit

Gene
N/A
Organism
Propionibacterium freudenreichii subsp. shermanii
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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 activityi

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

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTransferase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-12429
BRENDAi2.1.3.1 5032

Names & Taxonomyi

Protein namesi
Recommended name:
Methylmalonyl-CoA carboxyltransferase 12S subunit (EC:2.1.3.1)
Alternative name(s):
Transcarboxylase 12S subunit
OrganismiPropionibacterium freudenreichii subsp. shermanii
Taxonomic identifieri1752 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaPropionibacterialesPropionibacteriaceaePropionibacterium

Subcellular locationi

GO - Cellular componenti

Pathology & Biotechi

Chemistry databases

DrugBankiDB04183 Methylmalonic Acid
DB04045 Methylmalonyl-Coenzyme A

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001468172 – 611Methylmalonyl-CoA carboxyltransferase 12S subunitAdd BLAST610

Interactioni

Subunit structurei

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).

Structurei

Secondary structure

1611
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ8GBW6
SMRiQ8GBW6
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8GBW6

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini13 – 268CoA carboxyltransferase N-terminalPROSITE-ProRule annotationAdd BLAST256
Domaini274 – 506CoA carboxyltransferase C-terminalPROSITE-ProRule annotationAdd BLAST233

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni13 – 506CarboxyltransferasePROSITE-ProRule annotationAdd BLAST494

Phylogenomic databases

eggNOGiENOG4107QX3 Bacteria
COG4799 LUCA

Family and domain databases

InterProiView protein in InterPro
IPR034733 AcCoA_carboxyl
IPR000438 Acetyl_CoA_COase_Trfase_b_su
IPR029045 ClpP/crotonase-like_dom_sf
IPR011763 COA_CT_C
IPR011762 COA_CT_N
PfamiView protein in Pfam
PF01039 Carboxyl_trans, 1 hit
PRINTSiPR01070 ACCCTRFRASEB
SUPFAMiSSF52096 SSF52096, 2 hits
PROSITEiView protein in PROSITE
PS50989 COA_CT_CTER, 1 hit
PS50980 COA_CT_NTER, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8GBW6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAENNNLKLA STMEGRVEQL AEQRQVIEAG GGERRVEKQH SQGKQTARER
60 70 80 90 100
LNNLLDPHSF DEVGAFRKHR TTLFGMDKAV VPADGVVTGR GTILGRPVHA
110 120 130 140 150
ASQDFTVMGG SAGETQSTKV VETMEQALLT GTPFLFFYDS GGARIQEGID
160 170 180 190 200
SLSGYGKMFF ANVKLSGVVP QIAIIAGPCA GGASYSPALT DFIIMTKKAH
210 220 230 240 250
MFITGPQVIK SVTGEDVTAD ELGGAEAHMA ISGNIHFVAE DDDAAELIAK
260 270 280 290 300
KLLSFLPQNN TEEASFVNPN NDVSPNTELR DIVPIDGKKG YDVRDVIAKI
310 320 330 340 350
VDWGDYLEVK AGYATNLVTA FARVNGRSVG IVANQPSVMS GCLDINASDK
360 370 380 390 400
AAEFVNFCDS FNIPLVQLVD VPGFLPGVQQ EYGGIIRHGA KMLYAYSEAT
410 420 430 440 450
VPKITVVLRK AYGGSYLAMC NRDLGADAVY AWPSAEIAVM GAEGAANVIF
460 470 480 490 500
RKEIKAADDP DAMRAEKIEE YQNAFNTPYV AAARGQVDDV IDPADTRRKI
510 520 530 540 550
ASALEMYATK RQTRPAKKPW KLPLLSEEEI MADEEEKDLM IATLNKRVAS
560 570 580 590 600
LESELGSLQS DTQGVTEDVL TAISAVAAYL GNDGSAEVVH FAPSPNWVRE
610
GRRALQNHSI R
Length:611
Mass (Da):65,927
Last modified:January 23, 2007 - v3
Checksum:i625F1B284107B1FC
GO

Sequence cautioni

The sequence AAA25676 differs from that shown. Reason: Frameshift at several positions.Curated
The sequence CAD59919 differs from that shown. Reason: Frameshift at position 519.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti35R → L in AAA25676 (PubMed:8366018).Curated1
Sequence conflicti143Missing in AAA25676 (PubMed:8366018).Curated1
Sequence conflicti181 – 182GG → C in AAA25676 (PubMed:8366018).Curated2
Sequence conflicti377Missing in AAA25676 (PubMed:8366018).Curated1
Sequence conflicti390A → R in AAA25676 (PubMed:8366018).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04196 Genomic DNA Translation: AAA25676.1 Frameshift.
AJ535715 mRNA Translation: CAD59919.1 Frameshift.
PIRiA48665

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04196 Genomic DNA Translation: AAA25676.1 Frameshift.
AJ535715 mRNA Translation: CAD59919.1 Frameshift.
PIRiA48665

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ON3X-ray1.90A/B/C/D/E/F2-518[»]
1ON9X-ray2.00A/B/C/D/E/F2-518[»]
ProteinModelPortaliQ8GBW6
SMRiQ8GBW6
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

DrugBankiDB04183 Methylmalonic Acid
DB04045 Methylmalonyl-Coenzyme A

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4107QX3 Bacteria
COG4799 LUCA

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-12429
BRENDAi2.1.3.1 5032

Miscellaneous databases

EvolutionaryTraceiQ8GBW6

Family and domain databases

InterProiView protein in InterPro
IPR034733 AcCoA_carboxyl
IPR000438 Acetyl_CoA_COase_Trfase_b_su
IPR029045 ClpP/crotonase-like_dom_sf
IPR011763 COA_CT_C
IPR011762 COA_CT_N
PfamiView protein in Pfam
PF01039 Carboxyl_trans, 1 hit
PRINTSiPR01070 ACCCTRFRASEB
SUPFAMiSSF52096 SSF52096, 2 hits
PROSITEiView protein in PROSITE
PS50989 COA_CT_CTER, 1 hit
PS50980 COA_CT_NTER, 1 hit
ProtoNetiSearch...

Entry informationi

Entry namei12S_PROFR
AccessioniPrimary (citable) accession number: Q8GBW6
Secondary accession number(s): Q05617
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: January 23, 2007
Last modified: November 22, 2017
This is version 72 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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Main funding by: National Institutes of Health

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