Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q56185 (Q56185_STRWE) Unreviewed, UniProtKB/TrEMBL

Last modified September 21, 2011. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein names
Gene names
Name:fom4 EMBL BAA32491.1
OrganismStreptomyces wedmorensis EMBL BAA32491.1
Taxonomic identifier43759 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length198 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Metal binding1381Iron; via tele nitrogen PDB 1ZZ7 PDB 1ZZ8 PDB 1ZZ9
Metal binding1381Zinc; via tele nitrogen PDB 2BNM PDB 2BNN PDB 2BNO
Metal binding1421Iron PDB 1ZZ7 PDB 1ZZ8 PDB 1ZZ9
Metal binding1421Zinc PDB 2BNM PDB 2BNN PDB 2BNO
Metal binding1801Iron; via tele nitrogen PDB 1ZZ7 PDB 1ZZ8 PDB 1ZZ9
Metal binding1801Zinc; via tele nitrogen PDB 2BNM PDB 2BNN PDB 2BNO

Sequences

Sequence LengthMass (Da)Tools
Q56185 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 550D70A1D0D2FC56

FASTA19821,337
        10         20         30         40         50         60 
MSNTKTASTG FAELLKDRRE QVKMDHAALA SLLGETPETV AAWENGEGGE LTLTQLGRIA 

        70         80         90        100        110        120 
HVLGTSIGAL TPPAGNDLDD GVIIQMPDER PILKGVRDNV DYYVYNCLVR TKRAPSLVPL 

       130        140        150        160        170        180 
VVDVLTDNPD DAKFNSGHAG NEFLFVLEGE IHMKWGDKEN PKEALLPTGA SMFVEEHVPH 

       190 
AFTAAKGTGS AKLIAVNF 

« Hide

References

[1]"Sequence of a P-methyltransferase-encoding gene isolated from a bialaphos-producing Streptomyces hygroscopicus."
Hidaka T., Hidaka M., Kuzuyama T., Seto H.
Gene 158:149-150(1995) [PubMed: 7789803] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[2]"Nucleotide sequence of fortimicin KL1 methyltransferase gene isolated from Micromonospora olivasterospora, and comparison of its deduced amino acid sequence with those of methyltransferases involved in the biosynthesis of bialaphos and fosfomycin."
Kuzuyama T., Seki T., Dairi T., Hidaka T., Seto H.
J. Antibiot. 48:1191-1193(1995) [PubMed: 7490235] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[3]"Cloning and nucleotide sequence of fosfomycin biosynthetic genes of Streptomyces wedmorensis."
Hidaka T., Goda M., Kuzuyama T., Takei N., Hidaka M., Seto H.
Mol. Gen. Genet. 249:274-280(1995) [PubMed: 7500951] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[4]"Characterization of the fomA and fomB gene products from Streptomyces wedmorensis, which confer fosfomycin resistance on Escherichia coli."
Kobayashi S., Kuzuyama T., Seto H.
Antimicrob. Agents Chemother. 44:647-650(2000) [PubMed: 10681332] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[5]"Structure and reactivity of hydroxypropylphosphonic acid epoxidase in fosfomycin biosynthesis by a cation- and flavin-dependent mechanism."
McLuskey K., Cameron S., Hammerschmidt F., Hunter W.N.
Proc. Natl. Acad. Sci. U.S.A. 102:14221-14226(2005) [PubMed: 16186494] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH ZINC.
[6]"Structural insight into antibiotic fosfomycin biosynthesis by a mononuclear iron enzyme."
Higgins L.J., Yan F., Liu P., Liu H.W., Drennan C.L.
Nature 437:838-844(2005) [PubMed: 16015285] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH IRON.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB016934 Genomic DNA. Translation: BAA32491.1.
PIRS60215.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZZ6X-ray2.00A/B1-198[»]
1ZZ7X-ray2.10A/B1-198[»]
1ZZ8X-ray2.30A/B/C1-198[»]
1ZZ9X-ray2.40A/B/C1-198[»]
1ZZBX-ray2.30A/B1-198[»]
1ZZCX-ray1.80A/B1-198[»]
2BNMX-ray1.70A/B1-198[»]
2BNNX-ray2.50A/B1-198[»]
2BNOX-ray1.90A/B1-198[»]
3SCFX-ray2.85A/B/C1-198[»]
3SCGX-ray3.00A/B/C1-198[»]
3SCHX-ray2.10A/B1-198[»]
ProteinModelPortalQ56185.
SMRQ56185. Positions 5-198.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR013096. Cupin_2.
IPR011051. Cupin_RmlC_type.
IPR001387. HTH_3.
IPR010982. Lambda_DNA-bd.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
Gene3DG3DSA:1.10.260.40. G3DSA:1.10.260.40. 1 hit.
G3DSA:2.60.120.10. RmlC-like_jellyroll. 1 hit.
PfamPF07883. Cupin_2. 1 hit.
PF01381. HTH_3. 1 hit.
[Graphical view]
SMARTSM00530. HTH_XRE. 1 hit.
[Graphical view]
SUPFAMSSF47413. Lambda_like_DNA. 1 hit.
SSF51182. RmlC_like_cupin. 1 hit.
PROSITEPS50943. HTH_CROC1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ56185_STRWE
AccessionPrimary (citable) accession number: Q56185
Entry history
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: September 21, 2011
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)