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Protein

Methylmalonyl-CoA carboxyltransferase 12S subunit

Gene
N/A
Organism
Propionibacterium freudenreichii subsp. shermanii
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-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

Complete GO annotation...

Keywords - Molecular functioni

Transferase

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

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 611610Methylmalonyl-CoA carboxyltransferase 12S subunitPRO_0000146817Add
BLAST

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).

Protein-protein interaction databases

STRINGi754252.PFREUD_18860.

Structurei

Secondary structure

1
611
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi13 – 2816Combined sources
Turni29 – 313Combined sources
Helixi33 – 419Combined sources
Helixi47 – 548Combined sources
Beta strandi61 – 633Combined sources
Turni73 – 786Combined sources
Helixi82 – 854Combined sources
Beta strandi86 – 938Combined sources
Beta strandi96 – 1038Combined sources
Turni105 – 1073Combined sources
Helixi108 – 1103Combined sources
Helixi114 – 13017Combined sources
Beta strandi134 – 1407Combined sources
Helixi145 – 1484Combined sources
Helixi149 – 16517Combined sources
Turni166 – 1683Combined sources
Beta strandi171 – 18111Combined sources
Helixi182 – 1843Combined sources
Helixi185 – 1895Combined sources
Beta strandi190 – 1967Combined sources
Beta strandi200 – 2045Combined sources
Helixi206 – 2138Combined sources
Helixi219 – 2235Combined sources
Helixi225 – 2306Combined sources
Beta strandi236 – 2416Combined sources
Helixi242 – 25413Combined sources
Helixi277 – 2815Combined sources
Helixi294 – 3007Combined sources
Helixi302 – 3043Combined sources
Beta strandi306 – 3105Combined sources
Beta strandi317 – 3248Combined sources
Beta strandi327 – 3348Combined sources
Helixi339 – 3413Combined sources
Helixi345 – 36016Combined sources
Beta strandi365 – 3717Combined sources
Helixi378 – 3825Combined sources
Helixi385 – 39814Combined sources
Beta strandi403 – 41210Combined sources
Helixi413 – 4175Combined sources
Turni418 – 4203Combined sources
Helixi422 – 4243Combined sources
Beta strandi427 – 4315Combined sources
Beta strandi436 – 4405Combined sources
Helixi442 – 4498Combined sources
Helixi451 – 4566Combined sources
Beta strandi457 – 4593Combined sources
Helixi460 – 47516Combined sources
Helixi478 – 4836Combined sources
Beta strandi486 – 4905Combined sources
Helixi493 – 4953Combined sources
Helixi496 – 50611Combined sources
Helixi507 – 5093Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ON3X-ray1.90A/B/C/D/E/F2-518[»]
1ON9X-ray2.00A/B/C/D/E/F2-518[»]
ProteinModelPortaliQ8GBW6.
SMRiQ8GBW6. Positions 5-523.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8GBW6.

Family & Domainsi

Sequence similaritiesi

Contains 1 carboxyltransferase domain.Curated

Phylogenomic databases

eggNOGiENOG4107QX3. Bacteria.
COG4799. LUCA.

Family and domain databases

Gene3Di3.90.226.10. 2 hits.
InterProiIPR000438. Acetyl_CoA_COase_Trfase_b_su.
IPR000022. Carboxyl_trans.
IPR029045. ClpP/crotonase-like_dom.
IPR011763. COA_CT_C.
IPR011762. COA_CT_N.
[Graphical view]
PfamiPF01039. Carboxyl_trans. 1 hit.
[Graphical view]
PRINTSiPR01070. ACCCTRFRASEB.
SUPFAMiSSF52096. SSF52096. 2 hits.
PROSITEiPS50989. COA_CT_CTER. 1 hit.
PS50980. COA_CT_NTER. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 351R → L in AAA25676 (PubMed:8366018).Curated
Sequence conflicti143 – 1431Missing in AAA25676 (PubMed:8366018).Curated
Sequence conflicti181 – 1822GG → C in AAA25676 (PubMed:8366018).Curated
Sequence conflicti377 – 3771Missing in AAA25676 (PubMed:8366018).Curated
Sequence conflicti390 – 3901A → R in AAA25676 (PubMed:8366018).Curated

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.
RefSeqiWP_013161731.1. NZ_LN997841.1.

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.
RefSeqiWP_013161731.1. NZ_LN997841.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ON3X-ray1.90A/B/C/D/E/F2-518[»]
1ON9X-ray2.00A/B/C/D/E/F2-518[»]
ProteinModelPortaliQ8GBW6.
SMRiQ8GBW6. Positions 5-523.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi754252.PFREUD_18860.

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

Gene3Di3.90.226.10. 2 hits.
InterProiIPR000438. Acetyl_CoA_COase_Trfase_b_su.
IPR000022. Carboxyl_trans.
IPR029045. ClpP/crotonase-like_dom.
IPR011763. COA_CT_C.
IPR011762. COA_CT_N.
[Graphical view]
PfamiPF01039. Carboxyl_trans. 1 hit.
[Graphical view]
PRINTSiPR01070. ACCCTRFRASEB.
SUPFAMiSSF52096. SSF52096. 2 hits.
PROSITEiPS50989. COA_CT_CTER. 1 hit.
PS50980. COA_CT_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry namei12S_PROFR
AccessioniPrimary (citable) accession number: Q8GBW6
Secondary accession number(s): Q05617
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 62 of the entry and version 3 of the sequence. [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
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.