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Q70AC7

- 5S_PROFR

UniProt

Q70AC7 - 5S_PROFR

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Protein

Methylmalonyl-CoA carboxyltransferase 5S subunit

Gene
N/A
Organism
Propionibacterium freudenreichii subsp. shermanii
Status
Reviewed - 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 Co(2+) ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi23 – 231Cobalt
Binding sitei59 – 591Substrate; via amide nitrogen
Metal bindingi184 – 1841Cobalt
Binding sitei184 – 1841Substrate
Metal bindingi215 – 2151Cobalt
Metal bindingi217 – 2171Cobalt

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. methylmalonyl-CoA carboxytransferase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

Cobalt, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-12430.

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 lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesPropionibacterineaePropionibacteriaceaePropionibacterium

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi59 – 591A → T: Decreases activity by 96%. 1 Publication
Mutagenesisi184 – 1841K → A or E: Loss of activity. 1 Publication
Mutagenesisi186 – 1861M → I: Decreases activity by 98%. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 505505Methylmalonyl-CoA carboxyltransferase 5S subunitPRO_0000146816Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei184 – 1841N6-carboxylysine; partial1 Publication

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

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

Structurei

Secondary structure

1
505
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi11 – 133Combined sources
Beta strandi15 – 184Combined sources
Turni20 – 223Combined sources
Helixi23 – 286Combined sources
Helixi35 – 373Combined sources
Helixi39 – 413Combined sources
Helixi42 – 476Combined sources
Beta strandi51 – 577Combined sources
Helixi60 – 667Combined sources
Helixi72 – 8211Combined sources
Beta strandi88 – 925Combined sources
Helixi94 – 963Combined sources
Beta strandi99 – 1013Combined sources
Helixi105 – 11713Combined sources
Beta strandi122 – 1254Combined sources
Helixi133 – 14412Combined sources
Beta strandi148 – 1547Combined sources
Helixi163 – 17513Combined sources
Beta strandi179 – 1857Combined sources
Helixi192 – 20615Combined sources
Beta strandi212 – 2176Combined sources
Beta strandi219 – 2213Combined sources
Helixi223 – 23210Combined sources
Beta strandi236 – 2416Combined sources
Helixi243 – 2453Combined sources
Helixi254 – 2607Combined sources
Turni261 – 2633Combined sources
Beta strandi264 – 2674Combined sources
Helixi272 – 28514Combined sources
Helixi286 – 2927Combined sources
Helixi302 – 3054Combined sources
Helixi309 – 32012Combined sources
Turni325 – 3273Combined sources
Helixi328 – 34114Combined sources
Helixi351 – 36515Combined sources
Turni367 – 3693Combined sources
Helixi373 – 3797Combined sources
Turni380 – 3834Combined sources
Helixi392 – 40211Combined sources
Helixi411 – 4144Combined sources
Helixi419 – 4268Combined sources
Helixi436 – 4449Combined sources
Turni446 – 4483Combined sources
Helixi449 – 4557Combined sources
Helixi456 – 4583Combined sources
Helixi467 – 4737Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 3-474.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ70AC7.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni22 – 265Substrate binding

Sequence similaritiesi

Contains 1 carboxyltransferase domain.Curated

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 AAA03174.1 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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti341 – 3411A → AG in AAA03174. (PubMed:8365490)Curated
Sequence conflicti386 – 3861S → T in AAA03174. (PubMed:8365490)Curated
Sequence conflicti390 – 3901R → RDPKWSVGEEHRRAITQRPA DH in AAA03174. (PubMed:8365490)Curated
Sequence conflicti421 – 4211K → E in AAA03174. (PubMed:8365490)Curated
Sequence conflicti429 – 4291L → P in AAA03174. (PubMed:8365490)Curated
Sequence conflicti455 – 4551H → S in AAA03174. (PubMed:8365490)Curated
Sequence conflicti461 – 4611H → Q in AAA03174. (PubMed:8365490)Curated
Sequence conflicti481 – 4811L → V in AAA03174. (PubMed:8365490)Curated

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 .
PIRi S36808.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1RQB X-ray 1.90 A 2-505 [» ]
1RQE X-ray 2.50 A 2-505 [» ]
1RQH X-ray 2.00 A 2-505 [» ]
1RR2 X-ray 2.00 A 2-505 [» ]
1S3H X-ray 2.50 A 2-505 [» ]
1U5J X-ray 2.80 A 2-505 [» ]
ProteinModelPortali Q70AC7.
SMRi Q70AC7. Positions 3-474.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-12430.

Miscellaneous databases

EvolutionaryTracei Q70AC7.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
InterProi IPR013785. Aldolase_TIM.
IPR003379. Carboxylase_cons_dom.
IPR000891. PYR_CT.
[Graphical view ]
Pfami PF00682. HMGL-like. 1 hit.
PF02436. PYC_OADA. 1 hit.
[Graphical view ]
PROSITEi PS50991. PYR_CT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Primary structure of the 5 S subunit of transcarboxylase as deduced from the genomic DNA sequence."
    Thornton C.G., Kumar G.K., Shenoy B.C., Haase F.C., Phillips N.F.B., Park V.M., Magner W.J., Hejlik D.P., Wood H.G., Samols D.
    FEBS Lett. 330:191-196(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 3-22; 67-76; 88-92; 111-124; 134-147; 305-316; 325-337; 371-393; 397-410 AND 431-456.
    Strain: St33.
  2. "Expression and crystallization of several forms of the Propionibacterium shermanii transcarboxylase 5S subunit."
    Hall P.R., Zheng R., Pusztai-Carey M., van den Akker F., Carey P.R., Yee V.C.
    Acta Crystallogr. D 60:521-523(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 13673 / VPI 0409 / 33.
  3. "Transcarboxylase 5S structures: assembly and catalytic mechanism of a multienzyme complex subunit."
    Hall P.R., Zheng R., Antony L., Pusztai-Carey M., Carey P.R., Yee V.C.
    EMBO J. 23:3621-3631(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEXES WITH SUBSTRATE; PRODUCT AND COBALT IONS, SUBUNIT, CARBAMYLATION AT LYS-184, MUTAGENESIS OF ALA-59; LYS-184 AND MET-186.

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 26, 2014
This is version 47 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

External Data

Dasty 3