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P0C061

- GRSA_ANEMI

UniProt

P0C061 - GRSA_ANEMI

Protein

Gramicidin S synthase 1

Gene

grsA

Organism
Aneurinibacillus migulanus (Bacillus migulanus)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 54 (01 Oct 2014)
      Sequence version 1 (05 Jul 2005)
      Previous versions | rss
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    Functioni

    In the first step of peptide synthesis this enzyme activates phenylalanine and racemizes it to the D-isomer.

    Catalytic activityi

    ATP + L-phenylalanine + H2O = AMP + diphosphate + D-phenylalanine.

    Cofactori

    Binds 1 phosphopantetheine covalently.1 Publication

    Pathwayi

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. ligase activity Source: UniProtKB-KW
    3. phenylalanine racemase (ATP-hydrolyzing) activity Source: UniProtKB-EC

    GO - Biological processi

    1. antibiotic biosynthetic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Isomerase, Ligase

    Keywords - Biological processi

    Antibiotic biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-14128.
    UniPathwayiUPA00102.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Gramicidin S synthase 1
    Alternative name(s):
    Gramicidin S synthase I
    Including the following 2 domains:
    ATP-dependent D-phenylalanine adenylase
    Short name:
    D-PheA
    Alternative name(s):
    D-phenylalanine activase
    Phenylalanine racemase [ATP-hydrolyzing] (EC:5.1.1.11)
    Gene namesi
    Name:grsA
    Synonyms:grs1
    OrganismiAneurinibacillus migulanus (Bacillus migulanus)
    Taxonomic identifieri47500 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesPaenibacillaceaeAneurinibacillus groupAneurinibacillus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10981098Gramicidin S synthase 1PRO_0000193085Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei573 – 5731O-(pantetheine 4'-phosphoryl)serine1 PublicationPROSITE-ProRule annotation

    Keywords - PTMi

    Phosphopantetheine, Phosphoprotein

    Interactioni

    Subunit structurei

    Large multienzyme complex of GrsA and GrsB.

    Structurei

    Secondary structure

    1
    1098
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi20 – 278
    Helixi41 – 5111
    Beta strandi55 – 606
    Beta strandi63 – 664
    Helixi67 – 8317
    Beta strandi91 – 955
    Helixi100 – 11112
    Beta strandi115 – 1184
    Helixi125 – 13511
    Beta strandi138 – 1425
    Helixi144 – 1463
    Helixi147 – 1504
    Beta strandi157 – 1615
    Turni166 – 1694
    Beta strandi183 – 1908
    Beta strandi198 – 2047
    Helixi205 – 21612
    Beta strandi225 – 2284
    Helixi236 – 24510
    Turni246 – 2483
    Beta strandi250 – 2534
    Helixi256 – 2594
    Helixi262 – 27110
    Beta strandi276 – 2794
    Helixi281 – 2844
    Turni289 – 2913
    Beta strandi296 – 3038
    Helixi307 – 3137
    Turni314 – 3163
    Beta strandi317 – 3237
    Helixi326 – 3283
    Beta strandi332 – 3365
    Beta strandi349 – 3513
    Beta strandi355 – 3606
    Beta strandi372 – 3798
    Helixi390 – 3967
    Beta strandi397 – 3993
    Beta strandi401 – 4033
    Beta strandi406 – 41712
    Beta strandi423 – 4286
    Helixi429 – 4313
    Beta strandi432 – 4354
    Beta strandi438 – 4414
    Helixi442 – 4498
    Beta strandi455 – 46410
    Beta strandi470 – 48011
    Helixi484 – 49411
    Helixi497 – 4993
    Beta strandi502 – 5065
    Beta strandi516 – 5183
    Helixi520 – 5223

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AMUX-ray1.90A/B3-556[»]
    ProteinModelPortaliP0C061.
    SMRiP0C061. Positions 17-530.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0C061.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini543 – 60967Acyl carrierPROSITE-ProRule annotationAdd
    BLAST

    Domaini

    One-module-bearing peptide synthase with a C-terminal epimerization domain. Each module incorporates one amino acid into the peptide product and can be further subdivided into domains responsible for substrate adenylation, thiolation, condensation (not for the initiation module), and epimerization (optional), and N methylation (optional).

    Sequence similaritiesi

    Contains 1 acyl carrier domain.PROSITE-ProRule annotation

    Family and domain databases

    Gene3Di1.10.1200.10. 1 hit.
    InterProiIPR010071. AA_adenyl_domain.
    IPR009081. Acyl_carrier_prot-like.
    IPR025110. AMP-bd_C.
    IPR020845. AMP-binding_CS.
    IPR000873. AMP-dep_Synth/Lig.
    IPR001242. Condensatn.
    IPR010060. NRPS_synth.
    IPR006162. PPantetheine_attach_site.
    [Graphical view]
    PfamiPF00501. AMP-binding. 1 hit.
    PF13193. AMP-binding_C. 1 hit.
    PF00668. Condensation. 1 hit.
    PF00550. PP-binding. 1 hit.
    [Graphical view]
    SUPFAMiSSF47336. SSF47336. 1 hit.
    TIGRFAMsiTIGR01733. AA-adenyl-dom. 1 hit.
    TIGR01720. NRPS-para261. 1 hit.
    PROSITEiPS50075. ACP_DOMAIN. 1 hit.
    PS00455. AMP_BINDING. 1 hit.
    PS00012. PHOSPHOPANTETHEINE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0C061-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLNSSKSILI HAQNKNGTHE EEQYLFAVNN TKAEYPRDKT IHQLFEEQVS     50
    KRPNNVAIVC ENEQLTYHEL NVKANQLARI FIEKGIGKDT LVGIMMEKSI 100
    DLFIGILAVL KAGGAYVPID IEYPKERIQY ILDDSQARML LTQKHLVHLI 150
    HNIQFNGQVE IFEEDTIKIR EGTNLHVPSK STDLAYVIYT SGTTGNPKGT 200
    MLEHKGISNL KVFFENSLNV TEKDRIGQFA SISFDASVWE MFMALLTGAS 250
    LYIILKDTIN DFVKFEQYIN QKEITVITLP PTYVVHLDPE RILSIQTLIT 300
    AGSATSPSLV NKWKEKVTYI NAYGPTETTI CATTWVATKE TIGHSVPIGA 350
    PIQNTQIYIV DENLQLKSVG EAGELCIGGE GLARGYWKRP ELTSQKFVDN 400
    PFVPGEKLYK TGDQARWLSD GNIEYLGRID NQVKIRGHRV ELEEVESILL 450
    KHMYISETAV SVHKDHQEQP YLCAYFVSEK HIPLEQLRQF SSEELPTYMI 500
    PSYFIQLDKM PLTSNGKIDR KQLPEPDLTF GMRVDYEAPR NEIEETLVTI 550
    WQDVLGIEKI GIKDNFYALG GDSIKAIQVA ARLHSYQLKL ETKDLLKYPT 600
    IDQLVHYIKD SKRRSEQGIV EGEIGLTPIQ HWFFEQQFTN MHHWNQSYML 650
    YRPNGFDKEI LLRVFNKIVE HHDALRMIYK HHNGKIVQIN RGLEGTLFDF 700
    YTFDLTANDN EQQVICEESA RLQNSINLEV GPLVKIALFH TQNGDHLFMA 750
    IHHLVVDGIS WRILFEDLAT AYEQAMHQQT IALPEKTDSF KDWSIELEKY 800
    ANSELFLEEA EYWHHLNYYT ENVQIKKDYV TMNNKQKNIR YVGMELTIEE 850
    TEKLLKNVNK AYRTEINDIL LTALGFALKE WADIDKIVIN LEGHGREEIL 900
    EQMNIARTVG WFTSQYPVVL DMQKSDDLSY QIKLMKENLR RIPNKGIGYE 950
    IFKYLTTEYL RPVLPFTLKP EINFNYLGQF DTDVKTELFT RSPYSMGNSL 1000
    GPDGKNNLSP EGESYFVLNI NGFIEEGKLH ITFSYNEQQY KEDTIQQLSR 1050
    SYKQHLLAII EHCVQKEDTE LTPSDFSFKE LELEEMDDIF DLLADSLT 1098
    Length:1,098
    Mass (Da):126,632
    Last modified:July 5, 2005 - v1
    Checksum:iA4FD8282FE4AF2F4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti335 – 3351W → C in AAA58718. (PubMed:2477357)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M29703 Genomic DNA. Translation: AAA58718.1.
    X15577 Genomic DNA. Translation: CAA33603.1.
    PIRiJU0122. YGBSG1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M29703 Genomic DNA. Translation: AAA58718.1 .
    X15577 Genomic DNA. Translation: CAA33603.1 .
    PIRi JU0122. YGBSG1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AMU X-ray 1.90 A/B 3-556 [» ]
    ProteinModelPortali P0C061.
    SMRi P0C061. Positions 17-530.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00102 .
    BioCyci MetaCyc:MONOMER-14128.

    Miscellaneous databases

    EvolutionaryTracei P0C061.

    Family and domain databases

    Gene3Di 1.10.1200.10. 1 hit.
    InterProi IPR010071. AA_adenyl_domain.
    IPR009081. Acyl_carrier_prot-like.
    IPR025110. AMP-bd_C.
    IPR020845. AMP-binding_CS.
    IPR000873. AMP-dep_Synth/Lig.
    IPR001242. Condensatn.
    IPR010060. NRPS_synth.
    IPR006162. PPantetheine_attach_site.
    [Graphical view ]
    Pfami PF00501. AMP-binding. 1 hit.
    PF13193. AMP-binding_C. 1 hit.
    PF00668. Condensation. 1 hit.
    PF00550. PP-binding. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47336. SSF47336. 1 hit.
    TIGRFAMsi TIGR01733. AA-adenyl-dom. 1 hit.
    TIGR01720. NRPS-para261. 1 hit.
    PROSITEi PS50075. ACP_DOMAIN. 1 hit.
    PS00455. AMP_BINDING. 1 hit.
    PS00012. PHOSPHOPANTETHEINE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Gramicidin S biosynthesis operon containing the structural genes grsA and grsB has an open reading frame encoding a protein homologous to fatty acid thioesterases."
      Kraetzschmar J., Krause M., Marahiel M.A.
      J. Bacteriol. 171:5422-5429(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 9999 / DSM 2895 / JCM 8504 / NBRC 15520 / NCTC 7096.
    2. "Gramicidin S synthetase 1 (phenylalanine racemase), a prototype of amino acid racemases containing the cofactor 4'-phosphopantetheine."
      Stein T., Kluge B., Vater J., Franke P., Otto A., Wittmann-Liebold B.
      Biochemistry 34:4633-4642(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 564-575, COFACTOR, PHOSPHOPANTETHEINYLATION AT SER-573.
      Strain: ATCC 9999 / DSM 2895 / JCM 8504 / NBRC 15520 / NCTC 7096.
    3. "Structural basis for the activation of phenylalanine in the non-ribosomal biosynthesis of gramicidin S."
      Conti E., Stachelhaus T., Marahiel M.A., Brick P.
      EMBO J. 16:4174-4183(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 17-530, SEQUENCE REVISION TO 335.
      Strain: ATCC 9999 / DSM 2895 / JCM 8504 / NBRC 15520 / NCTC 7096.

    Entry informationi

    Entry nameiGRSA_ANEMI
    AccessioniPrimary (citable) accession number: P0C061
    Secondary accession number(s): P14687
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2005
    Last sequence update: July 5, 2005
    Last modified: October 1, 2014
    This is version 54 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The racemization reaction takes place in the thioester-bound stage of phenylalanine that is formed via the thiol group of the serine-bound phosphopantetheine.

    Keywords - Technical termi

    3D-structure, Direct protein sequencing, Multifunctional enzyme

    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

    External Data

    Dasty 3