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P0C061 (GRSA_ANEMI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Gramicidin S synthase 1
Alternative name(s):
Gramicidin S synthase I

Including the following 2 domains:

  1. ATP-dependent D-phenylalanine adenylase
    Short name=D-PheA
    Alternative name(s):
    D-phenylalanine activase
  2. Phenylalanine racemase [ATP-hydrolyzing]
    EC=5.1.1.11
Gene names
Name:grsA
Synonyms:grs1
OrganismAneurinibacillus migulanus (Bacillus migulanus)
Taxonomic identifier47500 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesPaenibacillaceaeAneurinibacillus groupAneurinibacillus

Protein attributes

Sequence length1098 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Binds 1 phosphopantetheine covalently. Ref.2

Pathway

Antibiotic biosynthesis; gramicidin S biosynthesis.

Subunit structure

Large multienzyme complex of GrsA and GrsB.

Domain

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).

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.

Sequence similarities

Belongs to the ATP-dependent AMP-binding enzyme family.

Contains 1 acyl carrier domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10981098Gramicidin S synthase 1
PRO_0000193085

Regions

Domain543 – 60967Acyl carrier

Amino acid modifications

Modified residue5731O-(pantetheine 4'-phosphoryl)serine

Experimental info

Sequence conflict3351W → C in AAA58718. Ref.1

Secondary structure

............................................................................................. 1098
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0C061 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: A4FD8282FE4AF2F4

FASTA1,098126,632
        10         20         30         40         50         60 
MLNSSKSILI HAQNKNGTHE EEQYLFAVNN TKAEYPRDKT IHQLFEEQVS KRPNNVAIVC 

        70         80         90        100        110        120 
ENEQLTYHEL NVKANQLARI FIEKGIGKDT LVGIMMEKSI DLFIGILAVL KAGGAYVPID 

       130        140        150        160        170        180 
IEYPKERIQY ILDDSQARML LTQKHLVHLI HNIQFNGQVE IFEEDTIKIR EGTNLHVPSK 

       190        200        210        220        230        240 
STDLAYVIYT SGTTGNPKGT MLEHKGISNL KVFFENSLNV TEKDRIGQFA SISFDASVWE 

       250        260        270        280        290        300 
MFMALLTGAS LYIILKDTIN DFVKFEQYIN QKEITVITLP PTYVVHLDPE RILSIQTLIT 

       310        320        330        340        350        360 
AGSATSPSLV NKWKEKVTYI NAYGPTETTI CATTWVATKE TIGHSVPIGA PIQNTQIYIV 

       370        380        390        400        410        420 
DENLQLKSVG EAGELCIGGE GLARGYWKRP ELTSQKFVDN PFVPGEKLYK TGDQARWLSD 

       430        440        450        460        470        480 
GNIEYLGRID NQVKIRGHRV ELEEVESILL KHMYISETAV SVHKDHQEQP YLCAYFVSEK 

       490        500        510        520        530        540 
HIPLEQLRQF SSEELPTYMI PSYFIQLDKM PLTSNGKIDR KQLPEPDLTF GMRVDYEAPR 

       550        560        570        580        590        600 
NEIEETLVTI WQDVLGIEKI GIKDNFYALG GDSIKAIQVA ARLHSYQLKL ETKDLLKYPT 

       610        620        630        640        650        660 
IDQLVHYIKD SKRRSEQGIV EGEIGLTPIQ HWFFEQQFTN MHHWNQSYML YRPNGFDKEI 

       670        680        690        700        710        720 
LLRVFNKIVE HHDALRMIYK HHNGKIVQIN RGLEGTLFDF YTFDLTANDN EQQVICEESA 

       730        740        750        760        770        780 
RLQNSINLEV GPLVKIALFH TQNGDHLFMA IHHLVVDGIS WRILFEDLAT AYEQAMHQQT 

       790        800        810        820        830        840 
IALPEKTDSF KDWSIELEKY ANSELFLEEA EYWHHLNYYT ENVQIKKDYV TMNNKQKNIR 

       850        860        870        880        890        900 
YVGMELTIEE TEKLLKNVNK AYRTEINDIL LTALGFALKE WADIDKIVIN LEGHGREEIL 

       910        920        930        940        950        960 
EQMNIARTVG WFTSQYPVVL DMQKSDDLSY QIKLMKENLR RIPNKGIGYE IFKYLTTEYL 

       970        980        990       1000       1010       1020 
RPVLPFTLKP EINFNYLGQF DTDVKTELFT RSPYSMGNSL GPDGKNNLSP EGESYFVLNI 

      1030       1040       1050       1060       1070       1080 
NGFIEEGKLH ITFSYNEQQY KEDTIQQLSR SYKQHLLAII EHCVQKEDTE LTPSDFSFKE 

      1090 
LELEEMDDIF DLLADSLT 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M29703 Genomic DNA. Translation: AAA58718.1.
X15577 Genomic DNA. Translation: CAA33603.1.
PIRYGBSG1. JU0122.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AMUX-ray1.90A/B3-556[»]
ProteinModelPortalP0C061.
SMRP0C061. Positions 17-530.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-14128.
UniPathwayUPA00102.

Family and domain databases

Gene3D1.10.1200.10. 1 hit.
InterProIPR010071. 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]
PfamPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
PF00668. Condensation. 1 hit.
PF00550. PP-binding. 1 hit.
[Graphical view]
SUPFAMSSF47336. SSF47336. 1 hit.
TIGRFAMsTIGR01733. AA-adenyl-dom. 1 hit.
TIGR01720. NRPS-para261. 1 hit.
PROSITEPS50075. ACP_DOMAIN. 1 hit.
PS00455. AMP_BINDING. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0C061.

Entry information

Entry nameGRSA_ANEMI
AccessionPrimary (citable) accession number: P0C061
Secondary accession number(s): P14687
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: July 5, 2005
Last modified: July 9, 2014
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways