SFMB_STRLA
ID SFMB_STRLA Reviewed; 1082 AA.
AC B0CN26;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Nonribosomal peptide synthase SfmB {ECO:0000305};
DE EC=6.2.1.66 {ECO:0000269|PubMed:17981978};
DE AltName: Full=Glycine--[glycyl-carrier protein] ligase {ECO:0000305};
GN Name=sfmB {ECO:0000303|PubMed:17981978};
OS Streptomyces lavendulae.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1914;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=NRRL 11002;
RX PubMed=17981978; DOI=10.1128/jb.00826-07;
RA Li L., Deng W., Song J., Ding W., Zhao Q.F., Peng C., Song W.W., Tang G.L.,
RA Liu W.;
RT "Characterization of the saframycin A gene cluster from Streptomyces
RT lavendulae NRRL 11002 revealing a nonribosomal peptide synthetase system
RT for assembling the unusual tetrapeptidyl skeleton in an iterative manner.";
RL J. Bacteriol. 190:251-263(2008).
CC -!- FUNCTION: Involved in the biosynthesis of saframycin A (SFM-A), a
CC potent antitumor antibiotic that belongs to the tetrahydroisoquinoline
CC family (PubMed:17981978). Specifically adenylates glycine and loads it
CC onto its peptidyl carrier domain, via a thioester linkage to the
CC phosphopanthetheine moiety (PubMed:17981978).
CC {ECO:0000269|PubMed:17981978}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + glycine + holo-[peptidyl-carrier protein] = AMP +
CC diphosphate + glycyl-[peptidyl-carrier protein];
CC Xref=Rhea:RHEA:61696, Rhea:RHEA-COMP:11480, Rhea:RHEA-COMP:15909,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:144951, ChEBI:CHEBI:456215;
CC EC=6.2.1.66; Evidence={ECO:0000269|PubMed:17981978};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61697;
CC Evidence={ECO:0000269|PubMed:17981978};
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000305};
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:17981978}.
CC -!- DISRUPTION PHENOTYPE: Inactivation of the gene completely abolishes the
CC ability to produce SFM-A. {ECO:0000269|PubMed:17981978}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; DQ838002; ABI22132.1; -; Genomic_DNA.
DR KEGG; ag:ABI22132; -.
DR BioCyc; MetaCyc:MON-19339; -.
DR BRENDA; 6.2.1.66; 133.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008610; P:lipid biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0030639; P:polyketide biosynthetic process; IEA:UniProt.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.30.559.10; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR029058; AB_hydrolase.
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; IPR042099; ANL_N_sf.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR020806; PKS_PP-bd.
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 SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW Antibiotic biosynthesis; Ligase; Phosphopantetheine; Phosphoprotein.
FT CHAIN 1..1082
FT /note="Nonribosomal peptide synthase SfmB"
FT /id="PRO_0000454780"
FT DOMAIN 951..1026
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 1027..1082
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1027..1041
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1043..1059
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 986
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 1082 AA; 115193 MW; F27CB4D0C395EE41 CRC64;
MNEMAGKAYG LAVRLDLRGA LERTALQSAL SAVVERHEAL RTGLRQIDGT LTQVVVPGVT
VSLPVVDLGG RGPDPAQLDR EVRRLARQEA QRGWNLAQPP LLRGLLARLA DDHHVLLLCV
HHAVCDGLSL QIVLRELLEN YTGGGPAGAD EPLQFADYVV WNNGGEEFPD PEWSARRQAA
REHWSSTLAG APQVLDLPTD RRRPPLQSYA GARVPVRLDT AFADRVRDWS AQRGVTPFTT
LLAAYTVVLA RNGGADDLLV GLPVANRSHA DLAGTVGYLA NTCPLRADLR ADPTLGELVR
DLYDRLTGVL EHADLPFGEL VELLAPPRMP ERNPVFQVMF GLQQDVRRGW DLPGLRVDVE
DVDCGNARVD LSLFLFEEAD GAIDGFLEYA SALFDRATAE RFADQLHTVL RQILRDARIP
VSAVDLVGNG SATTIDSFLD GGPLEQPWPL VWPRIRELAA RRPSAEAVRD DAEALDYASL
VDRVDAAAAR LTAAGAGPGD RVAVLAERGV RAVVAMLACW RAGGVYVPVD PAAPLPRREL
ILEQAAPAVL VCEDPDEQPP HHRSRAVAIG DLTAEADAGA GTPAEPAPRP HDPAYLMFTS
GSTGRPKGVA VSHANLSSFL HALTGRLALG PADRLLALTT TAFDISLLEL LGPLVTGGTV
VVAPSSAQRG AADLAARLSS PGITTAQATP AVWRLALSAG WRPREGFTLL CGGEALPPDL
ADLLAATPAE AHNLYGPTET TIWSCAARIR PGEPVTIGRP IPGTRVLVAD AALRPVPPGV
CGELLVGGPG VALGYLDDPA RTAARFVPDP YHPGERLYRT GDVVRLRSDG LIEFVGRVDE
QVKVRGHRIE LGEIESALRA LPGVRDAAAT VLDPRGNARI AGYLVADDGA LDTAGRAARL
RQDLSEALPA SMVPSELYAV PAIPLNPNGK VDRRALPGTG RRLEGGSERV APSTDAEHAV
AALWCELLSL PEVGVREDFF GLGGHSLLAA DLLQRLERDL GARVPVAEFF MEPTVARLAA
TVSQLSGAVH QTPTQDPDGR AEQTAEPSPE DRGADGDGWD FPTVRRSVTV PGSDPVPLEV
SP
