Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)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).

Protein-protein interaction databases

STRINGi754252.PFREUD_18860.

Structurei

Secondary structure

1611
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi13 – 28Combined sources16
Turni29 – 31Combined sources3
Helixi33 – 41Combined sources9
Helixi47 – 54Combined sources8
Beta strandi61 – 63Combined sources3
Turni73 – 78Combined sources6
Helixi82 – 85Combined sources4
Beta strandi86 – 93Combined sources8
Beta strandi96 – 103Combined sources8
Turni105 – 107Combined sources3
Helixi108 – 110Combined sources3
Helixi114 – 130Combined sources17
Beta strandi134 – 140Combined sources7
Helixi145 – 148Combined sources4
Helixi149 – 165Combined sources17
Turni166 – 168Combined sources3
Beta strandi171 – 181Combined sources11
Helixi182 – 184Combined sources3
Helixi185 – 189Combined sources5
Beta strandi190 – 196Combined sources7
Beta strandi200 – 204Combined sources5
Helixi206 – 213Combined sources8
Helixi219 – 223Combined sources5
Helixi225 – 230Combined sources6
Beta strandi236 – 241Combined sources6
Helixi242 – 254Combined sources13
Helixi277 – 281Combined sources5
Helixi294 – 300Combined sources7
Helixi302 – 304Combined sources3
Beta strandi306 – 310Combined sources5
Beta strandi317 – 324Combined sources8
Beta strandi327 – 334Combined sources8
Helixi339 – 341Combined sources3
Helixi345 – 360Combined sources16
Beta strandi365 – 371Combined sources7
Helixi378 – 382Combined sources5
Helixi385 – 398Combined sources14
Beta strandi403 – 412Combined sources10
Helixi413 – 417Combined sources5
Turni418 – 420Combined sources3
Helixi422 – 424Combined sources3
Beta strandi427 – 431Combined sources5
Beta strandi436 – 440Combined sources5
Helixi442 – 449Combined sources8
Helixi451 – 456Combined sources6
Beta strandi457 – 459Combined sources3
Helixi460 – 475Combined sources16
Helixi478 – 483Combined sources6
Beta strandi486 – 490Combined sources5
Helixi493 – 495Combined sources3
Helixi496 – 506Combined sources11
Helixi507 – 509Combined sources3

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...

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

Sequence similaritiesi

Contains 1 CoA carboxyltransferase C-terminal domain.PROSITE-ProRule annotation
Contains 1 CoA carboxyltransferase N-terminal domain.PROSITE-ProRule annotation

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)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...

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: November 2, 2016
This is version 64 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.