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Protein

Gramicidin S synthase 1

Gene

grsA

Organism
Aneurinibacillus migulanus (Bacillus migulanus)
Status
Reviewed-Annotation score: 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: gramicidin S biosynthesis

This protein is involved in the pathway gramicidin S biosynthesis, which is part of Antibiotic biosynthesis.
View all proteins of this organism that are known to be involved in the pathway gramicidin S biosynthesis and in Antibiotic biosynthesis.

GO - Molecular functioni

GO - Biological processi

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)DescriptionActionsGraphical viewLength
ChainiPRO_00001930851 – 1098Gramicidin S synthase 1Add BLAST1098

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei573O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1 Publication1

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Interactioni

Subunit structurei

Large multienzyme complex of GrsA and GrsB.

Structurei

Secondary structure

11098
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi20 – 27Combined sources8
Helixi41 – 51Combined sources11
Beta strandi55 – 60Combined sources6
Beta strandi63 – 66Combined sources4
Helixi67 – 83Combined sources17
Beta strandi91 – 95Combined sources5
Helixi100 – 111Combined sources12
Beta strandi115 – 118Combined sources4
Helixi125 – 135Combined sources11
Beta strandi138 – 142Combined sources5
Helixi144 – 146Combined sources3
Helixi147 – 150Combined sources4
Beta strandi157 – 161Combined sources5
Turni166 – 169Combined sources4
Beta strandi183 – 190Combined sources8
Beta strandi198 – 204Combined sources7
Helixi205 – 216Combined sources12
Beta strandi225 – 228Combined sources4
Helixi236 – 245Combined sources10
Turni246 – 248Combined sources3
Beta strandi250 – 253Combined sources4
Helixi256 – 259Combined sources4
Helixi262 – 271Combined sources10
Beta strandi276 – 279Combined sources4
Helixi281 – 284Combined sources4
Turni289 – 291Combined sources3
Beta strandi296 – 303Combined sources8
Helixi307 – 313Combined sources7
Turni314 – 316Combined sources3
Beta strandi317 – 323Combined sources7
Helixi326 – 328Combined sources3
Beta strandi332 – 336Combined sources5
Beta strandi349 – 351Combined sources3
Beta strandi355 – 360Combined sources6
Beta strandi372 – 379Combined sources8
Helixi390 – 396Combined sources7
Beta strandi397 – 399Combined sources3
Beta strandi401 – 403Combined sources3
Beta strandi406 – 417Combined sources12
Beta strandi423 – 428Combined sources6
Helixi429 – 431Combined sources3
Beta strandi432 – 435Combined sources4
Beta strandi438 – 441Combined sources4
Helixi442 – 449Combined sources8
Beta strandi455 – 464Combined sources10
Beta strandi470 – 480Combined sources11
Helixi484 – 494Combined sources11
Helixi497 – 499Combined sources3
Beta strandi502 – 506Combined sources5
Beta strandi516 – 518Combined sources3
Helixi520 – 522Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AMUX-ray1.90A/B3-556[»]
ProteinModelPortaliP0C061.
SMRiP0C061.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C061.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini543 – 609Acyl carrierPROSITE-ProRule annotationAdd BLAST67

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.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR001242. Condensatn.
IPR010060. NRPS_synth.
IPR009081. PP-bd_ACP.
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)DescriptionActionsGraphical viewLength
Sequence conflicti335W → C in AAA58718 (PubMed:2477357).Curated1

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.
RefSeqiWP_043064678.1. NZ_LGUG01000004.1.

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.
PIRiJU0122. YGBSG1.
RefSeqiWP_043064678.1. NZ_LGUG01000004.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AMUX-ray1.90A/B3-556[»]
ProteinModelPortaliP0C061.
SMRiP0C061.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00102.
BioCyciMetaCyc:MONOMER-14128.

Miscellaneous databases

EvolutionaryTraceiP0C061.

Family and domain databases

Gene3Di1.10.1200.10. 1 hit.
InterProiIPR010071. AA_adenyl_domain.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR001242. Condensatn.
IPR010060. NRPS_synth.
IPR009081. PP-bd_ACP.
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]
ProtoNetiSearch...

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 2, 2016
This is version 63 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

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.