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Q70AC7

- 5S_PROFR

UniProt

Q70AC7 - 5S_PROFR

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
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    • History
      Entry version 46 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    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

    Binds 1 Co2+ 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

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MSPREIEVSE PREVGITELV LRDAHQSLMA TRMAMEDMVG ACADIDAAGY    50
    WSVECWGGAT YDSCIRFLNE DPWERLRTFR KLMPNSRLQM LLRGQNLLGY 100
    RHYNDEVVDR FVDKSAENGM DVFRVFDAMN DPRNMAHAMA AVKKAGKHAQ 150
    GTICYTISPV HTVEGYVKLA GQLLDMGADS IALKDMAALL KPQPAYDIIK 200
    AIKDTYGQKT QINLHCHSTT GVTEVSLMKA IEAGVDVVDT AISSMSLGPG 250
    HNPTESVAEM LEGTGYTTNL DYDRLHKIRD HFKAIRPKYK KFESKTLVDT 300
    SIFKSQIPGG MLSNMESQLR AQGAEDKMDE VMAEVPRVRK AAGFPPLVTP 350
    SSQIVGTQAV FNVMMGEYKR MTGEFADIML GYYGASPADR DPKVVKLAEE 400
    QSGKKPITQR PADLLPPEWE KQSKEAATLK GFNGTDEDVL TYALFPQVAP 450
    VFFEHRAEGP HSVALTDAQL KAEAEGDEKS LAVAGPVTYN VNVGGTVREV 500
    TVQQA 505
    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.

    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L06488 Unassigned DNA. Translation: AAA03174.1. Frameshift.
    AJ606310 Genomic DNA. Translation: CAE54442.1.
    PIRiS36808.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L06488 Unassigned DNA. Translation: AAA03174.1 . Frameshift.
    AJ606310 Genomic DNA. Translation: CAE54442.1 .
    PIRi S36808.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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: October 1, 2014
    This is version 46 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