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Inosamine-phosphate amidinotransferase 1 (EC 2.1.4.2) (Aminocyclitol amidinotransferase) (ADT) (Inosamine-phosphate amidinotransferase I)

 STRB1_STRGR             Reviewed;         347 AA.
P08078;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
05-JUL-2017, entry version 92.
RecName: Full=Inosamine-phosphate amidinotransferase 1;
EC=2.1.4.2;
AltName: Full=Aminocyclitol amidinotransferase;
Short=ADT;
AltName: Full=Inosamine-phosphate amidinotransferase I;
Name=strB1; Synonyms=AT, strB;
Streptomyces griseus.
Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
Streptomyces.
NCBI_TaxID=1911;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=N2-3-11;
PubMed=3118332; DOI=10.1093/nar/15.19.8041;
Distler J., Ebert A., Mansouri K., Pissowotzki K., Stockmann M.,
Piepersberg W.;
"Gene cluster for streptomycin biosynthesis in Streptomyces griseus:
nucleotide sequence of three genes and analysis of transcriptional
activity.";
Nucleic Acids Res. 15:8041-8056(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-15.
STRAIN=ATCC 23345 / DSM 40236 / JCM 4644 / NBRC 12875 / NCIMB 13023 /
NRRL B-2682 / VKM Ac-800;
PubMed=3029728; DOI=10.1093/nar/15.4.1819;
Tohyama H., Okami Y., Umezawa H.;
"Nucleotide sequence of the streptomycinphosphotransferase and
amidinotransferase genes from Streptomyces griseus.";
Nucleic Acids Res. 15:1819-1833(1987).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 330-347.
PubMed=1654502; DOI=10.1007/BF00260640;
Mansouri K., Piepersberg W.;
"Genetics of streptomycin production in Streptomyces griseus:
nucleotide sequence of five genes, strFGHIK, including a phosphatase
gene.";
Mol. Gen. Genet. 228:459-469(1991).
[4]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS).
PubMed=9922132; DOI=10.1021/bi981949p;
Fritsche E., Bergner A., Humm A., Piepersberg W., Huber R.;
"Crystal structure of L-arginine:inosamine-phosphate
amidinotransferase StrB1 from Streptomyces griseus: an enzyme involved
in streptomycin biosynthesis.";
Biochemistry 37:17664-17672(1998).
-!- FUNCTION: Catalyzes two non-consecutive transamidination
reactions. It converts scyllo-inosamine 4-phosphate into N-
amidino-scyllo-inosamine 4-phosphate and N1-amidinostreptamine 6-
phosphate into streptidine 6-phosphate.
-!- CATALYTIC ACTIVITY: L-arginine + 1-amino-1-deoxy-scyllo-inositol
4-phosphate = L-ornithine + 1-guanidino-1-deoxy-scyllo-inositol 4-
phosphate.
-!- PATHWAY: Antibiotic biosynthesis; streptomycin biosynthesis.
-!- SUBUNIT: Homodimer.
-!- SIMILARITY: Belongs to the amidinotransferase family.
{ECO:0000305}.
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EMBL; Y00459; CAA68517.1; -; Genomic_DNA.
EMBL; X05045; CAA28718.1; -; Genomic_DNA.
PIR; B26984; B26984.
PDB; 1BWD; X-ray; 3.10 A; A/B=2-347.
PDBsum; 1BWD; -.
ProteinModelPortal; P08078; -.
SMR; P08078; -.
eggNOG; COG1834; LUCA.
BioCyc; MetaCyc:MONOMER-14013; -.
BRENDA; 2.1.4.2; 6035.
UniPathway; UPA00066; -.
EvolutionaryTrace; P08078; -.
GO; GO:0015069; F:scyllo-inosamine-4-phosphate amidinotransferase activity; IEA:UniProtKB-EC.
GO; GO:0019872; P:streptomycin biosynthetic process; IEA:UniProtKB-UniPathway.
InterPro; IPR033195; AmidinoTrfase.
PANTHER; PTHR10488; PTHR10488; 1.
1: Evidence at protein level;
3D-structure; Antibiotic biosynthesis; Direct protein sequencing;
Streptomycin biosynthesis; Transferase.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:3029728}.
CHAIN 2 347 Inosamine-phosphate amidinotransferase 1.
/FTId=PRO_0000215475.
ACT_SITE 179 179 {ECO:0000250}.
ACT_SITE 227 227
ACT_SITE 332 332 Amidino-cysteine intermediate.
VARIANT 144 146 SGS -> ERI (in strain: ISP 5236).
VARIANT 329 329 G -> R (in strain: ISP 5236).
VARIANT 340 342 TAR -> RPL (in strain: ISP 5236).
STRAND 8 11 {ECO:0000244|PDB:1BWD}.
STRAND 13 17 {ECO:0000244|PDB:1BWD}.
HELIX 31 36 {ECO:0000244|PDB:1BWD}.
TURN 37 41 {ECO:0000244|PDB:1BWD}.
HELIX 45 47 {ECO:0000244|PDB:1BWD}.
HELIX 55 74 {ECO:0000244|PDB:1BWD}.
STRAND 78 80 {ECO:0000244|PDB:1BWD}.
STRAND 87 89 {ECO:0000244|PDB:1BWD}.
HELIX 106 108 {ECO:0000244|PDB:1BWD}.
STRAND 109 119 {ECO:0000244|PDB:1BWD}.
HELIX 125 127 {ECO:0000244|PDB:1BWD}.
HELIX 130 134 {ECO:0000244|PDB:1BWD}.
HELIX 135 142 {ECO:0000244|PDB:1BWD}.
TURN 143 145 {ECO:0000244|PDB:1BWD}.
STRAND 147 150 {ECO:0000244|PDB:1BWD}.
HELIX 158 160 {ECO:0000244|PDB:1BWD}.
STRAND 173 175 {ECO:0000244|PDB:1BWD}.
HELIX 180 182 {ECO:0000244|PDB:1BWD}.
STRAND 183 186 {ECO:0000244|PDB:1BWD}.
STRAND 189 193 {ECO:0000244|PDB:1BWD}.
HELIX 200 210 {ECO:0000244|PDB:1BWD}.
STRAND 214 222 {ECO:0000244|PDB:1BWD}.
HELIX 228 230 {ECO:0000244|PDB:1BWD}.
STRAND 232 236 {ECO:0000244|PDB:1BWD}.
STRAND 239 242 {ECO:0000244|PDB:1BWD}.
TURN 244 246 {ECO:0000244|PDB:1BWD}.
TURN 249 251 {ECO:0000244|PDB:1BWD}.
HELIX 254 256 {ECO:0000244|PDB:1BWD}.
STRAND 259 263 {ECO:0000244|PDB:1BWD}.
STRAND 274 276 {ECO:0000244|PDB:1BWD}.
HELIX 281 285 {ECO:0000244|PDB:1BWD}.
STRAND 288 291 {ECO:0000244|PDB:1BWD}.
STRAND 294 298 {ECO:0000244|PDB:1BWD}.
HELIX 302 310 {ECO:0000244|PDB:1BWD}.
STRAND 314 318 {ECO:0000244|PDB:1BWD}.
HELIX 323 326 {ECO:0000244|PDB:1BWD}.
TURN 330 333 {ECO:0000244|PDB:1BWD}.
STRAND 335 340 {ECO:0000244|PDB:1BWD}.
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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