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Protein

Methylmalonyl-CoA carboxyltransferase 5S subunit

Gene
N/A
Organism
Propionibacterium freudenreichii subsp. shermanii
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The 5S subunit specifically catalyzes the transfer of the carboxyl group from biotin of the 1.3S subunit to pyruvate to form oxaloacetate and 1.3S biotin.

Catalytic activityi

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

Cofactori

Co2+Note: Binds 1 Co2+ ion per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi23Cobalt1
Binding sitei59Substrate; via amide nitrogen1
Metal bindingi184Cobalt1
Binding sitei184Substrate1
Metal bindingi215Cobalt1
Metal bindingi217Cobalt1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

Cobalt, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-12430.
BRENDAi2.1.3.1. 5032.

Names & Taxonomyi

Protein namesi
Recommended name:
Methylmalonyl-CoA carboxyltransferase 5S subunit (EC:2.1.3.1)
Alternative name(s):
Transcarboxylase 5S subunit
OrganismiPropionibacterium freudenreichii subsp. shermanii
Taxonomic identifieri1752 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaPropionibacterialesPropionibacteriaceaePropionibacterium

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi59A → T: Decreases activity by 96%. 1 Publication1
Mutagenesisi184K → A or E: Loss of activity. 1 Publication1
Mutagenesisi186M → I: Decreases activity by 98%. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001468161 – 505Methylmalonyl-CoA carboxyltransferase 5S subunitAdd BLAST505

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei184N6-carboxylysine; partial1 Publication1

Post-translational modificationi

Lys-184 is carbamylated in the free enzyme and helps to coordinate the cobalt ion. Lys-184 is partially carbamylated in the complex with pyruvate, but is not carbamylated in the oxaloacetate-bound form.1 Publication

Proteomic databases

PRIDEiQ70AC7.

Interactioni

Subunit structurei

Homodimer. 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_18870.

Structurei

Secondary structure

1505
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi11 – 13Combined sources3
Beta strandi15 – 18Combined sources4
Turni20 – 22Combined sources3
Helixi23 – 28Combined sources6
Helixi35 – 37Combined sources3
Helixi39 – 41Combined sources3
Helixi42 – 47Combined sources6
Beta strandi51 – 57Combined sources7
Helixi60 – 66Combined sources7
Helixi72 – 82Combined sources11
Beta strandi88 – 92Combined sources5
Helixi94 – 96Combined sources3
Beta strandi99 – 101Combined sources3
Helixi105 – 117Combined sources13
Beta strandi122 – 125Combined sources4
Helixi133 – 144Combined sources12
Beta strandi148 – 154Combined sources7
Helixi163 – 175Combined sources13
Beta strandi179 – 185Combined sources7
Helixi192 – 206Combined sources15
Beta strandi212 – 217Combined sources6
Beta strandi219 – 221Combined sources3
Helixi223 – 232Combined sources10
Beta strandi236 – 241Combined sources6
Helixi243 – 245Combined sources3
Helixi254 – 260Combined sources7
Turni261 – 263Combined sources3
Beta strandi264 – 267Combined sources4
Helixi272 – 285Combined sources14
Helixi286 – 292Combined sources7
Helixi302 – 305Combined sources4
Helixi309 – 320Combined sources12
Turni325 – 327Combined sources3
Helixi328 – 341Combined sources14
Helixi351 – 365Combined sources15
Turni367 – 369Combined sources3
Helixi373 – 379Combined sources7
Turni380 – 383Combined sources4
Helixi392 – 402Combined sources11
Helixi411 – 414Combined sources4
Helixi419 – 426Combined sources8
Helixi436 – 444Combined sources9
Turni446 – 448Combined sources3
Helixi449 – 455Combined sources7
Helixi456 – 458Combined sources3
Helixi467 – 473Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RQBX-ray1.90A2-505[»]
1RQEX-ray2.50A2-505[»]
1RQHX-ray2.00A2-505[»]
1RR2X-ray2.00A2-505[»]
1S3HX-ray2.50A2-505[»]
1U5JX-ray2.80A2-505[»]
ProteinModelPortaliQ70AC7.
SMRiQ70AC7.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ70AC7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini14 – 276Pyruvate carboxyltransferasePROSITE-ProRule annotationAdd BLAST263

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni22 – 26Substrate binding5

Sequence similaritiesi

Contains 1 pyruvate carboxyltransferase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4107QSA. Bacteria.
COG5016. LUCA.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR003379. Carboxylase_cons_dom.
IPR000891. PYR_CT.
[Graphical view]
PfamiPF00682. HMGL-like. 1 hit.
PF02436. PYC_OADA. 1 hit.
[Graphical view]
PROSITEiPS50991. PYR_CT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q70AC7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPREIEVSE PREVGITELV LRDAHQSLMA TRMAMEDMVG ACADIDAAGY
60 70 80 90 100
WSVECWGGAT YDSCIRFLNE DPWERLRTFR KLMPNSRLQM LLRGQNLLGY
110 120 130 140 150
RHYNDEVVDR FVDKSAENGM DVFRVFDAMN DPRNMAHAMA AVKKAGKHAQ
160 170 180 190 200
GTICYTISPV HTVEGYVKLA GQLLDMGADS IALKDMAALL KPQPAYDIIK
210 220 230 240 250
AIKDTYGQKT QINLHCHSTT GVTEVSLMKA IEAGVDVVDT AISSMSLGPG
260 270 280 290 300
HNPTESVAEM LEGTGYTTNL DYDRLHKIRD HFKAIRPKYK KFESKTLVDT
310 320 330 340 350
SIFKSQIPGG MLSNMESQLR AQGAEDKMDE VMAEVPRVRK AAGFPPLVTP
360 370 380 390 400
SSQIVGTQAV FNVMMGEYKR MTGEFADIML GYYGASPADR DPKVVKLAEE
410 420 430 440 450
QSGKKPITQR PADLLPPEWE KQSKEAATLK GFNGTDEDVL TYALFPQVAP
460 470 480 490 500
VFFEHRAEGP HSVALTDAQL KAEAEGDEKS LAVAGPVTYN VNVGGTVREV

TVQQA
Length:505
Mass (Da):55,649
Last modified:July 5, 2004 - v1
Checksum:i6DF657E231609064
GO

Sequence cautioni

The sequence AAA03174 differs from that shown. Reason: Frameshift at positions 205, 217, 340, 344, 360, 426, 428, 457, 460, 463, 474, 480, 494 and 499.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti341A → AG in AAA03174 (PubMed:8365490).Curated1
Sequence conflicti386S → T in AAA03174 (PubMed:8365490).Curated1
Sequence conflicti390R → RDPKWSVGEEHRRAITQRPA DH in AAA03174 (PubMed:8365490).Curated1
Sequence conflicti421K → E in AAA03174 (PubMed:8365490).Curated1
Sequence conflicti429L → P in AAA03174 (PubMed:8365490).Curated1
Sequence conflicti455H → S in AAA03174 (PubMed:8365490).Curated1
Sequence conflicti461H → Q in AAA03174 (PubMed:8365490).Curated1
Sequence conflicti481L → V in AAA03174 (PubMed:8365490).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06488 Unassigned DNA. Translation: AAA03174.1. Frameshift.
AJ606310 Genomic DNA. Translation: CAE54442.1.
PIRiS36808.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06488 Unassigned DNA. Translation: AAA03174.1. Frameshift.
AJ606310 Genomic DNA. Translation: CAE54442.1.
PIRiS36808.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RQBX-ray1.90A2-505[»]
1RQEX-ray2.50A2-505[»]
1RQHX-ray2.00A2-505[»]
1RR2X-ray2.00A2-505[»]
1S3HX-ray2.50A2-505[»]
1U5JX-ray2.80A2-505[»]
ProteinModelPortaliQ70AC7.
SMRiQ70AC7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi754252.PFREUD_18870.

Proteomic databases

PRIDEiQ70AC7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4107QSA. Bacteria.
COG5016. LUCA.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-12430.
BRENDAi2.1.3.1. 5032.

Miscellaneous databases

EvolutionaryTraceiQ70AC7.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR003379. Carboxylase_cons_dom.
IPR000891. PYR_CT.
[Graphical view]
PfamiPF00682. HMGL-like. 1 hit.
PF02436. PYC_OADA. 1 hit.
[Graphical view]
PROSITEiPS50991. PYR_CT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry namei5S_PROFR
AccessioniPrimary (citable) accession number: Q70AC7
Secondary accession number(s): Q05618
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: July 5, 2004
Last modified: November 2, 2016
This is version 55 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.