GRSA_BREBE
ID GRSA_BREBE Reviewed; 1098 AA.
AC P0C062; P14687;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Gramicidin S synthase 1;
DE AltName: Full=Gramicidin S synthase I;
DE Includes:
DE RecName: Full=ATP-dependent D-phenylalanine adenylase;
DE Short=D-PheA;
DE AltName: Full=D-phenylalanine activase;
DE Includes:
DE RecName: Full=Phenylalanine racemase [ATP-hydrolyzing];
DE EC=5.1.1.11;
GN Name=grsA; Synonyms=grs1;
OS Brevibacillus brevis (Bacillus brevis).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=1393;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Nagano;
RX PubMed=2691508; DOI=10.1093/oxfordjournals.jbchem.a122909;
RA Hori K., Yamamoto Y., Minetoki T., Kurotsu T., Kanda M., Miura S.,
RA Okamura K., Furuyama J., Saito Y.;
RT "Molecular cloning and nucleotide sequence of the gramicidin S synthetase 1
RT gene.";
RL J. Biochem. 106:639-645(1989).
CC -!- FUNCTION: In the first step of peptide synthesis this enzyme activates
CC phenylalanine and racemizes it to the D-isomer. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-phenylalanine = AMP + D-phenylalanine +
CC diphosphate + H(+); Xref=Rhea:RHEA:20201, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57981, ChEBI:CHEBI:58095, ChEBI:CHEBI:456215;
CC EC=5.1.1.11;
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000250};
CC Note=Binds 1 phosphopantetheine covalently. {ECO:0000250};
CC -!- PATHWAY: Antibiotic biosynthesis; gramicidin S biosynthesis.
CC -!- SUBUNIT: Large multienzyme complex of GrsA and GrsB. {ECO:0000250}.
CC -!- DOMAIN: One-module-bearing peptide synthase with a C-terminal
CC epimerization domain. Each module incorporates one amino acid into the
CC peptide product and can be further subdivided into domains responsible
CC for substrate adenylation, thiolation, condensation (not for the
CC initiation module), and epimerization (optional), and N methylation
CC (optional) (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: The racemization reaction takes place in the thioester-
CC bound stage of phenylalanine that is formed via the thiol group of the
CC serine-bound phosphopantetheine. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D00519; BAA00406.1; -; Genomic_DNA.
DR EMBL; D00938; BAA00777.1; -; Genomic_DNA.
DR PIR; JU0122; YGBSG1.
DR PDB; 5ISW; X-ray; 1.75 A; A=538-1098.
DR PDB; 5ISX; X-ray; 2.33 A; A/B=538-1098.
DR PDBsum; 5ISW; -.
DR PDBsum; 5ISX; -.
DR AlphaFoldDB; P0C062; -.
DR SMR; P0C062; -.
DR KEGG; ag:BAA00406; -.
DR BRENDA; 5.1.1.11; 638.
DR SABIO-RK; P0C062; -.
DR UniPathway; UPA00102; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0047462; F:phenylalanine racemase (ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.30.559.10; -; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR010060; NRPS_synth.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR TIGRFAMs; TIGR01720; NRPS-para261; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; ATP-binding; Isomerase; Ligase;
KW Multifunctional enzyme; Nucleotide-binding; Phosphopantetheine;
KW Phosphoprotein.
FT CHAIN 1..1098
FT /note="Gramicidin S synthase 1"
FT /id="PRO_0000193086"
FT DOMAIN 538..612
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 573
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT HELIX 540..555
FT /evidence="ECO:0007829|PDB:5ISW"
FT TURN 566..570
FT /evidence="ECO:0007829|PDB:5ISW"
FT HELIX 573..584
FT /evidence="ECO:0007829|PDB:5ISW"
FT TURN 585..587
FT /evidence="ECO:0007829|PDB:5ISW"
FT HELIX 592..597
FT /evidence="ECO:0007829|PDB:5ISW"
FT HELIX 601..604
FT /evidence="ECO:0007829|PDB:5ISW"
FT HELIX 605..607
FT /evidence="ECO:0007829|PDB:5ISW"
FT STRAND 622..624
FT /evidence="ECO:0007829|PDB:5ISW"
FT HELIX 628..636
FT /evidence="ECO:0007829|PDB:5ISW"
FT TURN 639..642
FT /evidence="ECO:0007829|PDB:5ISW"
FT STRAND 644..652
FT /evidence="ECO:0007829|PDB:5ISW"
FT HELIX 658..671
FT /evidence="ECO:0007829|PDB:5ISW"
FT HELIX 673..676
FT /evidence="ECO:0007829|PDB:5ISW"
FT STRAND 677..682
FT /evidence="ECO:0007829|PDB:5ISW"
FT STRAND 685..690
FT /evidence="ECO:0007829|PDB:5ISW"
FT STRAND 699..704
FT /evidence="ECO:0007829|PDB:5ISW"
FT HELIX 711..723
FT /evidence="ECO:0007829|PDB:5ISW"
FT TURN 728..730
FT /evidence="ECO:0007829|PDB:5ISW"
FT STRAND 734..741
FT /evidence="ECO:0007829|PDB:5ISW"
FT STRAND 744..752
FT /evidence="ECO:0007829|PDB:5ISW"
FT HELIX 753..755
FT /evidence="ECO:0007829|PDB:5ISW"
FT HELIX 758..776
FT /evidence="ECO:0007829|PDB:5ISW"
FT HELIX 790..800
FT /evidence="ECO:0007829|PDB:5ISW"
FT HELIX 804..807
FT /evidence="ECO:0007829|PDB:5ISW"
FT HELIX 808..818
FT /evidence="ECO:0007829|PDB:5ISW"
FT HELIX 836..838
FT /evidence="ECO:0007829|PDB:5ISW"
FT STRAND 839..845
FT /evidence="ECO:0007829|PDB:5ISW"
FT HELIX 848..856
FT /evidence="ECO:0007829|PDB:5ISW"
FT TURN 859..863
FT /evidence="ECO:0007829|PDB:5ISW"
FT HELIX 866..882
FT /evidence="ECO:0007829|PDB:5ISW"
FT STRAND 885..893
FT /evidence="ECO:0007829|PDB:5ISW"
FT STRAND 900..902
FT /evidence="ECO:0007829|PDB:5ISX"
FT STRAND 914..921
FT /evidence="ECO:0007829|PDB:5ISW"
FT HELIX 928..939
FT /evidence="ECO:0007829|PDB:5ISW"
FT HELIX 943..946
FT /evidence="ECO:0007829|PDB:5ISW"
FT HELIX 948..954
FT /evidence="ECO:0007829|PDB:5ISW"
FT TURN 958..960
FT /evidence="ECO:0007829|PDB:5ISW"
FT STRAND 971..979
FT /evidence="ECO:0007829|PDB:5ISW"
FT HELIX 981..984
FT /evidence="ECO:0007829|PDB:5ISW"
FT STRAND 1017..1025
FT /evidence="ECO:0007829|PDB:5ISW"
FT STRAND 1028..1036
FT /evidence="ECO:0007829|PDB:5ISW"
FT TURN 1037..1039
FT /evidence="ECO:0007829|PDB:5ISW"
FT HELIX 1042..1065
FT /evidence="ECO:0007829|PDB:5ISW"
SQ SEQUENCE 1098 AA; 126566 MW; B8E0B55C33BBA1E8 CRC64;
MLNSSKSILI HAQNKNGTHE EEQYLFAVNN TKAEYPRDKT IHQLFEEQVS KRPNNVAIVC
ENEQLTYHEL NVKANQLARI FIEKGIGKDT LVGIMMEKSI DLFIGILAVL KAGGAYVPID
IEYPKERIQY ILDDSQARML LTQKHLVHLI HNIQFNGQVE IFEEDTIKIR EGTNLHVPSK
STDLAYVIYT SGTTGNPKGT MLEHKGISNL KVFFENSLNV TEKDRIGQFA SISFDASVWE
MFMALLTGAS LYIILKDTIN DFVKFEQYIN QKEITVITLP PTYVVHLDPE RILSIQTLIT
AGSATSPSLV NKWKEKVTYI NAYGPTETTI CATTWVATKE TTGHSVPIGA PIQNTQIYIV
DENLQLKSVG EAGELCIGGE GLARGYWKRP ELTSQKFVDN PFVPGEKLYK TGDQARWLPD
GNIEYLGRID NQVKIRGHRV ELEEVESILL KHMYISETAV SVHKDHQEQP YLCAIFVSEK
HIPLEQLRQF SSEELPTYMI PSYFIQLDKM PLTSNGKIDR KQLPEPDLTF GMRVDYEAPR
NEIEETLVTI WQDVLGIEKI GIKDNFYALG GDSIKAIQVA ARLHSYQLKL ETKDLLKYPT
IDQLVHYIKD SKRRSEQGIV EGEIGLTPIQ HWFFEQQFTN MHHWNQSYML YRPNGFDKEI
LLRVFNKIVE HHDALRMIYK HHNGKIVQIN RGLEGTLFDF YTFDLTANDN EQQVICEESA
RLQNSINLEV GPLVKIALFH TQNGDHLFMA IHHLVVDGIS WRILFEDLAT AYEQAMHQQT
IALPEKTDSF KDWSIELEKY ANSELFLEEA EYWHHLNYYT DNVQIKKDYV TMNNKQKNIR
YVGMELTIEE TEKLLKNVNK AYRTEINDIL LTALGFALKE WADIDKIVIN LEGHGREEIL
EQMNIARTVG WFTSQYPVVL DMQKSDDLSY QIKLMKENLR RIPNKGIGYE IFKYLTTEYL
RPVLPFTLKP EINFNYLGQF DTDVKTELFT RSPYSMGNSL GPDGKNNLSP EGESYFVLNI
NGFIEEGKLH ITFSYNEQQY KEDTIQQLSR SYKQHLLAII EHCVQKEDTE LTPSDFSFKE
LELEEMDDIF DLLADSLT
