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STRB1_STRGR
ID   STRB1_STRGR             Reviewed;         347 AA.
AC   P08078;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Inosamine-phosphate amidinotransferase 1;
DE            EC=2.1.4.2;
DE   AltName: Full=Aminocyclitol amidinotransferase;
DE            Short=ADT;
DE   AltName: Full=Inosamine-phosphate amidinotransferase I;
GN   Name=strB1; Synonyms=AT, strB;
OS   Streptomyces griseus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=N2-3-11;
RX   PubMed=3118332; DOI=10.1093/nar/15.19.8041;
RA   Distler J., Ebert A., Mansouri K., Pissowotzki K., Stockmann M.,
RA   Piepersberg W.;
RT   "Gene cluster for streptomycin biosynthesis in Streptomyces griseus:
RT   nucleotide sequence of three genes and analysis of transcriptional
RT   activity.";
RL   Nucleic Acids Res. 15:8041-8056(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-15.
RC   STRAIN=ATCC 23345 / DSM 40236 / JCM 4644 / NBRC 12875 / NCIMB 13023 / NRRL
RC   B-2682 / VKM Ac-800 / IMRU 3463;
RX   PubMed=3029728; DOI=10.1093/nar/15.4.1819;
RA   Tohyama H., Okami Y., Umezawa H.;
RT   "Nucleotide sequence of the streptomycinphosphotransferase and
RT   amidinotransferase genes from Streptomyces griseus.";
RL   Nucleic Acids Res. 15:1819-1833(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 330-347.
RX   PubMed=1654502; DOI=10.1007/bf00260640;
RA   Mansouri K., Piepersberg W.;
RT   "Genetics of streptomycin production in Streptomyces griseus: nucleotide
RT   sequence of five genes, strFGHIK, including a phosphatase gene.";
RL   Mol. Gen. Genet. 228:459-469(1991).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS).
RX   PubMed=9922132; DOI=10.1021/bi981949p;
RA   Fritsche E., Bergner A., Humm A., Piepersberg W., Huber R.;
RT   "Crystal structure of L-arginine:inosamine-phosphate amidinotransferase
RT   StrB1 from Streptomyces griseus: an enzyme involved in streptomycin
RT   biosynthesis.";
RL   Biochemistry 37:17664-17672(1998).
CC   -!- FUNCTION: Catalyzes two non-consecutive transamidination reactions. It
CC       converts scyllo-inosamine 4-phosphate into N-amidino-scyllo-inosamine
CC       4-phosphate and N1-amidinostreptamine 6-phosphate into streptidine 6-
CC       phosphate.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-amino-1-deoxy-scyllo-inositol 4-phosphate + L-arginine = 1-
CC         guanidino-1-deoxy-scyllo-inositol 4-phosphate + L-ornithine;
CC         Xref=Rhea:RHEA:13265, ChEBI:CHEBI:32682, ChEBI:CHEBI:46911,
CC         ChEBI:CHEBI:57656, ChEBI:CHEBI:58325; EC=2.1.4.2;
CC   -!- PATHWAY: Antibiotic biosynthesis; streptomycin biosynthesis.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the amidinotransferase family. {ECO:0000305}.
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DR   EMBL; Y00459; CAA68517.1; -; Genomic_DNA.
DR   EMBL; X05045; CAA28718.1; -; Genomic_DNA.
DR   PIR; B26984; B26984.
DR   PDB; 1BWD; X-ray; 3.10 A; A/B=2-347.
DR   PDBsum; 1BWD; -.
DR   AlphaFoldDB; P08078; -.
DR   SMR; P08078; -.
DR   BioCyc; MetaCyc:MON-14013; -.
DR   BRENDA; 2.1.4.2; 6035.
DR   UniPathway; UPA00066; -.
DR   EvolutionaryTrace; P08078; -.
DR   GO; GO:0015069; F:scyllo-inosamine-4-phosphate amidinotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019872; P:streptomycin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR033195; AmidinoTrfase.
DR   PANTHER; PTHR10488; PTHR10488; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic biosynthesis; Direct protein sequencing;
KW   Streptomycin biosynthesis; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:3029728"
FT   CHAIN           2..347
FT                   /note="Inosamine-phosphate amidinotransferase 1"
FT                   /id="PRO_0000215475"
FT   ACT_SITE        179
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        227
FT   ACT_SITE        332
FT                   /note="Amidino-cysteine intermediate"
FT   VARIANT         144..146
FT                   /note="SGS -> ERI (in strain: ISP 5236)"
FT   VARIANT         329
FT                   /note="G -> R (in strain: ISP 5236)"
FT   VARIANT         340..342
FT                   /note="TAR -> RPL (in strain: ISP 5236)"
FT   STRAND          8..11
FT                   /evidence="ECO:0007829|PDB:1BWD"
FT   STRAND          13..17
FT                   /evidence="ECO:0007829|PDB:1BWD"
FT   HELIX           31..36
FT                   /evidence="ECO:0007829|PDB:1BWD"
FT   TURN            37..41
FT                   /evidence="ECO:0007829|PDB:1BWD"
FT   HELIX           45..47
FT                   /evidence="ECO:0007829|PDB:1BWD"
FT   HELIX           55..74
FT                   /evidence="ECO:0007829|PDB:1BWD"
FT   STRAND          78..80
FT                   /evidence="ECO:0007829|PDB:1BWD"
FT   STRAND          87..89
FT                   /evidence="ECO:0007829|PDB:1BWD"
FT   HELIX           106..108
FT                   /evidence="ECO:0007829|PDB:1BWD"
FT   STRAND          109..119
FT                   /evidence="ECO:0007829|PDB:1BWD"
FT   HELIX           125..127
FT                   /evidence="ECO:0007829|PDB:1BWD"
FT   HELIX           130..134
FT                   /evidence="ECO:0007829|PDB:1BWD"
FT   HELIX           135..142
FT                   /evidence="ECO:0007829|PDB:1BWD"
FT   TURN            143..145
FT                   /evidence="ECO:0007829|PDB:1BWD"
FT   STRAND          147..150
FT                   /evidence="ECO:0007829|PDB:1BWD"
FT   HELIX           158..160
FT                   /evidence="ECO:0007829|PDB:1BWD"
FT   STRAND          173..175
FT                   /evidence="ECO:0007829|PDB:1BWD"
FT   HELIX           180..182
FT                   /evidence="ECO:0007829|PDB:1BWD"
FT   STRAND          183..186
FT                   /evidence="ECO:0007829|PDB:1BWD"
FT   STRAND          189..193
FT                   /evidence="ECO:0007829|PDB:1BWD"
FT   HELIX           200..210
FT                   /evidence="ECO:0007829|PDB:1BWD"
FT   STRAND          214..222
FT                   /evidence="ECO:0007829|PDB:1BWD"
FT   HELIX           228..230
FT                   /evidence="ECO:0007829|PDB:1BWD"
FT   STRAND          232..236
FT                   /evidence="ECO:0007829|PDB:1BWD"
FT   STRAND          239..242
FT                   /evidence="ECO:0007829|PDB:1BWD"
FT   TURN            244..246
FT                   /evidence="ECO:0007829|PDB:1BWD"
FT   TURN            249..251
FT                   /evidence="ECO:0007829|PDB:1BWD"
FT   HELIX           254..256
FT                   /evidence="ECO:0007829|PDB:1BWD"
FT   STRAND          259..263
FT                   /evidence="ECO:0007829|PDB:1BWD"
FT   STRAND          274..276
FT                   /evidence="ECO:0007829|PDB:1BWD"
FT   HELIX           281..285
FT                   /evidence="ECO:0007829|PDB:1BWD"
FT   STRAND          288..291
FT                   /evidence="ECO:0007829|PDB:1BWD"
FT   STRAND          294..298
FT                   /evidence="ECO:0007829|PDB:1BWD"
FT   HELIX           302..310
FT                   /evidence="ECO:0007829|PDB:1BWD"
FT   STRAND          314..318
FT                   /evidence="ECO:0007829|PDB:1BWD"
FT   HELIX           323..326
FT                   /evidence="ECO:0007829|PDB:1BWD"
FT   TURN            330..333
FT                   /evidence="ECO:0007829|PDB:1BWD"
FT   STRAND          335..340
FT                   /evidence="ECO:0007829|PDB:1BWD"
SQ   SEQUENCE   347 AA;  38656 MW;  E92868467BD7BC1A CRC64;
     MSLVSVHNEW DPLEEVIVGT AVGARVPTAD RSVFAVEYAG DYESQEQIPS GAYPDRVLKE
     TEEELHVLAA ELTKLGVTVR RPGPRDHSAL IKTPDWETDG FHDYCPRDGL LSVGQTIIET
     PMALRSRFLE SLAYKDLLLE YFASGSRWLS APKPRLTDDS YAPQAPAGER LTDEEPVFDA
     ANVLRFGTDL LYLVSDSGNE LGAKWLQSAV GDTYTVHPCR KLYASTHVDS TIVPLRPGLV
     LTNPSRVNDE NMPDFLRSWE NITCPELVDI GFTGDKPHCS VWIGMNLLVV RPDLAVVDRR
     QTALIRLLEK HGMNVLPLQL THSRTLGGGF HCATLDVRRT ARETYQF
 
 
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