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P0C061

- GRSA_ANEMI

UniProt

P0C061 - GRSA_ANEMI

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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

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

pantetheine 4'-phosphate1 PublicationNote: 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
Complete GO annotation...

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MLNSSKSILI HAQNKNGTHE EEQYLFAVNN TKAEYPRDKT IHQLFEEQVS
60 70 80 90 100
KRPNNVAIVC ENEQLTYHEL NVKANQLARI FIEKGIGKDT LVGIMMEKSI
110 120 130 140 150
DLFIGILAVL KAGGAYVPID IEYPKERIQY ILDDSQARML LTQKHLVHLI
160 170 180 190 200
HNIQFNGQVE IFEEDTIKIR EGTNLHVPSK STDLAYVIYT SGTTGNPKGT
210 220 230 240 250
MLEHKGISNL KVFFENSLNV TEKDRIGQFA SISFDASVWE MFMALLTGAS
260 270 280 290 300
LYIILKDTIN DFVKFEQYIN QKEITVITLP PTYVVHLDPE RILSIQTLIT
310 320 330 340 350
AGSATSPSLV NKWKEKVTYI NAYGPTETTI CATTWVATKE TIGHSVPIGA
360 370 380 390 400
PIQNTQIYIV DENLQLKSVG EAGELCIGGE GLARGYWKRP ELTSQKFVDN
410 420 430 440 450
PFVPGEKLYK TGDQARWLSD GNIEYLGRID NQVKIRGHRV ELEEVESILL
460 470 480 490 500
KHMYISETAV SVHKDHQEQP YLCAYFVSEK HIPLEQLRQF SSEELPTYMI
510 520 530 540 550
PSYFIQLDKM PLTSNGKIDR KQLPEPDLTF GMRVDYEAPR NEIEETLVTI
560 570 580 590 600
WQDVLGIEKI GIKDNFYALG GDSIKAIQVA ARLHSYQLKL ETKDLLKYPT
610 620 630 640 650
IDQLVHYIKD SKRRSEQGIV EGEIGLTPIQ HWFFEQQFTN MHHWNQSYML
660 670 680 690 700
YRPNGFDKEI LLRVFNKIVE HHDALRMIYK HHNGKIVQIN RGLEGTLFDF
710 720 730 740 750
YTFDLTANDN EQQVICEESA RLQNSINLEV GPLVKIALFH TQNGDHLFMA
760 770 780 790 800
IHHLVVDGIS WRILFEDLAT AYEQAMHQQT IALPEKTDSF KDWSIELEKY
810 820 830 840 850
ANSELFLEEA EYWHHLNYYT ENVQIKKDYV TMNNKQKNIR YVGMELTIEE
860 870 880 890 900
TEKLLKNVNK AYRTEINDIL LTALGFALKE WADIDKIVIN LEGHGREEIL
910 920 930 940 950
EQMNIARTVG WFTSQYPVVL DMQKSDDLSY QIKLMKENLR RIPNKGIGYE
960 970 980 990 1000
IFKYLTTEYL RPVLPFTLKP EINFNYLGQF DTDVKTELFT RSPYSMGNSL
1010 1020 1030 1040 1050
GPDGKNNLSP EGESYFVLNI NGFIEEGKLH ITFSYNEQQY KEDTIQQLSR
1060 1070 1080 1090
SYKQHLLAII EHCVQKEDTE LTPSDFSFKE LELEEMDDIF DLLADSLT
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:
EMBLi
GenBanki
DDBJi
Links Updated
M29703 Genomic DNA. Translation: AAA58718.1.
X15577 Genomic DNA. Translation: CAA33603.1.
PIRiJU0122. YGBSG1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M29703 Genomic DNA. Translation: AAA58718.1 .
X15577 Genomic DNA. Translation: CAA33603.1 .
PIRi JU0122. YGBSG1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 55 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