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Protein

Methylmalonyl-CoA carboxyltransferase 1.3S subunit

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

Functioni

The biotinyl 1.3S subunit serves as a carboxyl carrier between the substrate-binding sites on the 12S and 5S subunits.

Catalytic activityi

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

GO - Molecular functioni

Keywordsi

Molecular functionTransferase
LigandBiotin

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-12431

Names & Taxonomyi

Protein namesi
Recommended name:
Methylmalonyl-CoA carboxyltransferase 1.3S subunit (EC:2.1.3.1)
Alternative name(s):
Biotin carboxyl carrier protein of transcarboxylase
Transcarboxylase, 1.3S subunit
OrganismiPropionibacterium freudenreichii subsp. shermanii
Taxonomic identifieri1752 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaPropionibacterialesPropionibacteriaceaePropionibacterium

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi87A → M: Reduces activity 10-fold; when associated with L-88. 1 Publication1
Mutagenesisi88M → A, C, T or L: Reduces activity at least 10-fold. 1 Publication1
Mutagenesisi90M → L: No effect. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001468091 – 123Methylmalonyl-CoA carboxyltransferase 1.3S subunitAdd BLAST123

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei89N6-biotinyllysinePROSITE-ProRule annotation1 Publication1

Proteomic databases

PRIDEiP02904

Interactioni

Subunit structurei

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).1 Publication

Structurei

Secondary structure

1123
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi54 – 62Combined sources9
Beta strandi64 – 68Combined sources5
Beta strandi80 – 87Combined sources8
Beta strandi90 – 95Combined sources6
Beta strandi97 – 105Combined sources9
Beta strandi117 – 122Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DCZNMR-A47-123[»]
1DD2NMR-A47-123[»]
1O78NMR-A1-9[»]
A51-123[»]
ProteinModelPortaliP02904
SMRiP02904
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02904

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini46 – 123Biotinyl-bindingPROSITE-ProRule annotationAdd BLAST78

Phylogenomic databases

eggNOGiENOG4105PV1 Bacteria
COG0511 LUCA

Family and domain databases

InterProiView protein in InterPro
IPR001882 Biotin_BS
IPR000089 Biotin_lipoyl
IPR011053 Single_hybrid_motif
PfamiView protein in Pfam
PF00364 Biotin_lipoyl, 1 hit
SUPFAMiSSF51230 SSF51230, 1 hit
PROSITEiView protein in PROSITE
PS00188 BIOTIN, 1 hit
PS50968 BIOTINYL_LIPOYL, 1 hit

Sequencei

Sequence statusi: Complete.

P02904-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLKVTVNGT AYDVDVDVDK SHENPMGTIL FGGGTGGAPA PRAAGGAGAG
60 70 80 90 100
KAGEGEIPAP LAGTVSKILV KEGDTVKAGQ TVLVLEAMKM ETEINAPTDG
110 120
KVEKVLVKER DAVQGGQGLI KIG
Length:123
Mass (Da):12,367
Last modified:July 21, 1986 - v1
Checksum:iD0980C2065EA9A89
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11738 Genomic DNA Translation: AAA25674.1
PIRiA03401 BKIP
RefSeqiWP_013161729.1, NZ_LN997841.1

Genome annotation databases

GeneIDi29491824

Similar proteinsi

Entry informationi

Entry nameiBCCP_PROFR
AccessioniPrimary (citable) accession number: P02904
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 23, 2018
This is version 110 of the entry and version 1 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

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