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