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Protein

Methylmalonyl-CoA carboxyltransferase 1.3S 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 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

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

Biotin

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi87 – 871A → M: Reduces activity 10-fold; when associated with L-88. 1 Publication
Mutagenesisi88 – 881M → A, C, T or L: Reduces activity at least 10-fold. 1 Publication
Mutagenesisi90 – 901M → L: No effect. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 123123Methylmalonyl-CoA carboxyltransferase 1.3S subunitPRO_0000146809Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei89 – 891N6-biotinyllysinePROSITE-ProRule annotation1 Publication

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

Protein-protein interaction databases

STRINGi754252.PFREUD_18840.

Structurei

Secondary structure

1
123
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi54 – 629Combined sources
Beta strandi64 – 685Combined sources
Beta strandi80 – 878Combined sources
Beta strandi90 – 956Combined sources
Beta strandi97 – 1059Combined sources
Beta strandi117 – 1226Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DCZNMR-A47-123[»]
1DD2NMR-A47-123[»]
1O78NMR-A1-123[»]
ProteinModelPortaliP02904.
SMRiP02904. Positions 48-123.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02904.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini46 – 12378Biotinyl-bindingPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 biotinyl-binding domain.PROSITE-ProRule annotationCurated

Phylogenomic databases

eggNOGiENOG4105PV1. Bacteria.
COG0511. LUCA.

Family and domain databases

InterProiIPR001882. Biotin_BS.
IPR000089. Biotin_lipoyl.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF00364. Biotin_lipoyl. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
PROSITEiPS00188. BIOTIN. 1 hit.
PS50968. BIOTINYL_LIPOYL. 1 hit.
[Graphical view]

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.

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DCZNMR-A47-123[»]
1DD2NMR-A47-123[»]
1O78NMR-A1-123[»]
ProteinModelPortaliP02904.
SMRiP02904. Positions 48-123.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi754252.PFREUD_18840.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105PV1. Bacteria.
COG0511. LUCA.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-12431.

Miscellaneous databases

EvolutionaryTraceiP02904.

Family and domain databases

InterProiIPR001882. Biotin_BS.
IPR000089. Biotin_lipoyl.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF00364. Biotin_lipoyl. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
PROSITEiPS00188. BIOTIN. 1 hit.
PS50968. BIOTINYL_LIPOYL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiBCCP_PROFR
AccessioniPrimary (citable) accession number: P02904
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 6, 2016
This is version 103 of the entry and version 1 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.