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Protein

GDP-perosamine synthase

Gene

per

Organism
Caulobacter crescentus (strain ATCC 19089 / CB15)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the synthesis of GDP-perosamine from GDP-4-keto-6-deoxy-D-mannose and L-glutamate. Can use only L-glutamate as amino donor. In vitro, can also use GDP-4-keto-3,6-dideoxymannose to produce GDP-3-deoxyperosamine. Involved in the formation of S-LPS, which is required for attachment of the protein S-layer to the outer membrane surface.3 Publications

Catalytic activityi

GDP-4-amino-4,6-dideoxy-alpha-D-mannose + 2-oxoglutarate = GDP-4-dehydro-6-deoxy-alpha-D-mannose + L-glutamate.2 Publications

Cofactori

pyridoxal 5'-phosphate2 Publications

Kineticsi

kcat is 2.7 sec(-1) for GDP-4-keto-6-deoxy-D-mannose. kcat is 0.015 sec(-1) for GDP-4-keto-3,6-dideoxymannose.1 Publication

Manual assertion based on experiment ini

  1. KM=0.013 mM for GDP-4-keto-6-deoxy-D-mannose1 Publication
  2. KM=0.016 mM for GDP-4-keto-3,6-dideoxymannose1 Publication
  3. KM=4.6 mM for L-glutamate (with GDP-4-keto-6-deoxy-D-mannose as cosubstrate)1 Publication
  4. KM=0.13 mM for L-glutamate (with GDP-4-keto-3,6-dideoxymannose as cosubstrate)1 Publication

    Pathwayi: LPS O-antigen biosynthesis

    This protein is involved in the pathway LPS O-antigen biosynthesis, which is part of Bacterial outer membrane biogenesis.1 Publication
    View all proteins of this organism that are known to be involved in the pathway LPS O-antigen biosynthesis and in Bacterial outer membrane biogenesis.

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Aminotransferase, Transferase

    Keywords - Biological processi

    Lipopolysaccharide biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BRENDAi2.6.1.102. 1218.
    UniPathwayiUPA00281.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    GDP-perosamine synthase2 Publications (EC:2.6.1.1022 Publications)
    Gene namesi
    Name:per1 Publication
    Ordered Locus Names:CC_1012Imported
    OrganismiCaulobacter crescentus (strain ATCC 19089 / CB15)
    Taxonomic identifieri190650 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaCaulobacteralesCaulobacteraceaeCaulobacter
    Proteomesi
    • UP000001816 Componenti: Chromosome

    Pathology & Biotechi

    Disruption phenotypei

    Mutant produces altered S-LPS.1 Publication

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi186K → A: Loss of activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004307191 – 371GDP-perosamine synthaseAdd BLAST371

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei186N6-(pyridoxal phosphate)lysine1 PublicationBy similarity1

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi190650.CC_1012.

    Structurei

    Secondary structure

    1371
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi18 – 28Combined sources11
    Helixi36 – 49Combined sources14
    Beta strandi52 – 59Combined sources8
    Helixi60 – 71Combined sources12
    Beta strandi78 – 85Combined sources8
    Helixi88 – 95Combined sources8
    Beta strandi99 – 103Combined sources5
    Turni107 – 109Combined sources3
    Helixi114 – 116Combined sources3
    Helixi118 – 120Combined sources3
    Beta strandi125 – 128Combined sources4
    Helixi133 – 135Combined sources3
    Helixi140 – 149Combined sources10
    Beta strandi153 – 157Combined sources5
    Beta strandi173 – 181Combined sources9
    Beta strandi186 – 188Combined sources3
    Beta strandi194 – 199Combined sources6
    Helixi201 – 211Combined sources11
    Helixi234 – 245Combined sources12
    Helixi247 – 265Combined sources19
    Helixi266 – 268Combined sources3
    Beta strandi271 – 273Combined sources3
    Beta strandi286 – 292Combined sources7
    Helixi300 – 309Combined sources10
    Helixi321 – 323Combined sources3
    Helixi325 – 330Combined sources6
    Helixi336 – 344Combined sources9
    Beta strandi345 – 348Combined sources4
    Helixi356 – 367Combined sources12

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3BN1X-ray1.80A/B/C/D2-371[»]
    3DR4X-ray1.60A/B/C/D1-371[»]
    3DR7X-ray1.70A/B/C/D1-371[»]
    ProteinModelPortaliQ9A9H3.
    SMRiQ9A9H3.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9A9H3.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the DegT/DnrJ/EryC1 family.Curated

    Phylogenomic databases

    eggNOGiENOG4105CF4. Bacteria.
    COG0399. LUCA.
    HOGENOMiHOG000230163.
    KOiK13010.
    OMAiMTGTIGH.

    Family and domain databases

    CDDicd00616. AHBA_syn. 1 hit.
    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProiIPR000653. DegT/StrS_aminotransferase.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view]
    PfamiPF01041. DegT_DnrJ_EryC1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000390. PLP_StrS. 1 hit.
    SUPFAMiSSF53383. SSF53383. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9A9H3-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSDLPRISVA APRLDGNERD YVLECMDTTW ISSVGRFIVE FEKAFADYCG
    60 70 80 90 100
    VKHAIACNNG TTALHLALVA MGIGPGDEVI VPSLTYIASA NSVTYCGATP
    110 120 130 140 150
    VLVDNDPRTF NLDAAKLEAL ITPRTKAIMP VHLYGQICDM DPILEVARRH
    160 170 180 190 200
    NLLVIEDAAE AVGATYRGKK SGSLGDCATF SFFGNKIITT GEGGMITTND
    210 220 230 240 250
    DDLAAKMRLL RGQGMDPNRR YWFPIVGFNY RMTNIQAAIG LAQLERVDEH
    260 270 280 290 300
    LAARERVVGW YEQKLARLGN RVTKPHVALT GRHVFWMYTV RLGEGLSTTR
    310 320 330 340 350
    DQVIKDLDAL GIESRPVFHP MHIMPPYAHL ATDDLKIAEA CGVDGLNLPT
    360 370
    HAGLTEADID RVIAALDQVL V
    Length:371
    Mass (Da):40,637
    Last modified:June 1, 2001 - v1
    Checksum:iAA4205787508C427
    GO

    Sequence cautioni

    The sequence AAC38670 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF062345 Genomic DNA. Translation: AAC38670.2. Different initiation.
    AE005673 Genomic DNA. Translation: AAK22996.1.
    PIRiH87374.
    RefSeqiNP_419828.1. NC_002696.2.
    WP_010918896.1. NC_002696.2.

    Genome annotation databases

    EnsemblBacteriaiAAK22996; AAK22996; CC_1012.
    GeneIDi940730.
    KEGGiccr:CC_1012.
    PATRICi21299000. VBICauCre124313_1030.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF062345 Genomic DNA. Translation: AAC38670.2. Different initiation.
    AE005673 Genomic DNA. Translation: AAK22996.1.
    PIRiH87374.
    RefSeqiNP_419828.1. NC_002696.2.
    WP_010918896.1. NC_002696.2.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3BN1X-ray1.80A/B/C/D2-371[»]
    3DR4X-ray1.60A/B/C/D1-371[»]
    3DR7X-ray1.70A/B/C/D1-371[»]
    ProteinModelPortaliQ9A9H3.
    SMRiQ9A9H3.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi190650.CC_1012.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAK22996; AAK22996; CC_1012.
    GeneIDi940730.
    KEGGiccr:CC_1012.
    PATRICi21299000. VBICauCre124313_1030.

    Phylogenomic databases

    eggNOGiENOG4105CF4. Bacteria.
    COG0399. LUCA.
    HOGENOMiHOG000230163.
    KOiK13010.
    OMAiMTGTIGH.

    Enzyme and pathway databases

    UniPathwayiUPA00281.
    BRENDAi2.6.1.102. 1218.

    Miscellaneous databases

    EvolutionaryTraceiQ9A9H3.

    Family and domain databases

    CDDicd00616. AHBA_syn. 1 hit.
    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProiIPR000653. DegT/StrS_aminotransferase.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view]
    PfamiPF01041. DegT_DnrJ_EryC1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000390. PLP_StrS. 1 hit.
    SUPFAMiSSF53383. SSF53383. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiGDPPS_CAUCR
    AccessioniPrimary (citable) accession number: Q9A9H3
    Secondary accession number(s): O85354
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 29, 2014
    Last sequence update: June 1, 2001
    Last modified: November 2, 2016
    This is version 81 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, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. 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.