Iron(3+)-hydroxamate-binding protein fhuD (P07822)

Identification
Name:Iron(3+)-hydroxamate-binding protein fhuD
Synonyms:
  • Ferric hydroxamate uptake protein D
  • Ferrichrome-binding periplasmic protein
  • Iron(III)-hydroxamate-binding protein fhuD
Gene Name:fhuD
Enzyme Class:Not Available
Biological Properties
General Function:Involved in binding
Specific Function:Part of the ABC transporter complex fhuCDB involved in iron(3+)-hydroxamate import. Binds the iron(3+)-hydroxamate complex and transfers it to the membrane-bound permease. Required for the transport of all iron(3+)-hydroxamate siderophores such as ferrichrome, gallichrome, desferrioxamine, coprogen, aerobactin, shizokinen, rhodotorulic acid and the antibiotic albomycin
Cellular Location:Periplasm
SMPDB Pathways:Not Available
KEGG Pathways:
Complex Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Water + 1.0Ferric coprogen → 1.0ADP + 1.0Ferric coprogen + 1.0Hydrogen ion + 1.0Phosphate
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Water + 1.0Aerobactin → 1.0ADP + 1.0Aerobactin + 1.0Hydrogen ion + 1.0Phosphate
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Water + 1.0Ferrichrome → 1.0ADP + 1.0Ferrichrome + 1.0Hydrogen ion + 1.0Phosphate
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Water + 1.0Ferroxamine → 1.0ADP + 1.0Ferroxamine + 1.0Hydrogen ion + 1.0Phosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB21185AerobactinMetaboCard
ECMDB20516Ferric coprogenMetaboCard
ECMDB21218FerrichromeMetaboCard
ECMDB21217Ferrichrome minus Fe(III)MetaboCard
ECMDB21333FerroxamineMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
cation transmembrane transporter activity
di-, tri-valent inorganic cation transmembrane transporter activity
inorganic cation transmembrane transporter activity
ion transmembrane transporter activity
iron ion transmembrane transporter activity
substrate-specific transmembrane transporter activity
transmembrane transporter activity
transporter activity
Process
cation transport
establishment of localization
high-affinity iron ion transport
ion transport
iron ion transmembrane transport
iron ion transport
metal ion transport
transition metal ion transport
transport
Gene Properties
Blattner:b0152
Gene OrientationClockwise
Centisome Percentage:3.68
Left Sequence End170575
Right Sequence End171465
Gene Sequence:
>891 bp
ATGAGCGGCTTACCTCTTATTTCGCGCCGTCGACTGTTAACGGCGATGGCGCTTTCTCCG
TTGTTATGGCAGATGAATACCGCCCACGCGGCGGCTATTGATCCCAATCGTATTGTGGCG
CTGGAGTGGTTGCCGGTGGAATTACTGCTGGCGCTCGGCATCGTGCCTTACGGCGTGGCG
GATACCATCAACTATCGCCTGTGGGTCAGCGAACCACCATTGCCGGACTCAGTGATCGAC
GTCGGTTTGCGCACAGAACCTAACCTTGAACTGCTGACCGAAATGAAACCATCGTTTATG
GTCTGGTCGGCAGGATATGGCCCTTCACCAGAAATGCTGGCTCGTATTGCGCCGGGTCGC
GGATTTAACTTCAGTGACGGCAAACAGCCGTTGGCGATGGCGCGTAAATCGCTGACGGAA
ATGGCAGATTTACTTAACCTGCAAAGCGCAGCGGAAACGCATTTAGCGCAATATGAAGAC
TTTATCCGCAGCATGAAACCCCGCTTTGTGAAGCGTGGTGCGCGTCCGTTATTGCTGACG
ACGCTTATCGATCCGCGCCATATGCTGGTCTTCGGTCCAAACAGCTTGTTCCAGGAAATT
CTTGATGAGTACGGCATCCCAAATGCCTGGCAAGGGGAAACCAACTTCTGGGGCAGTACC
GCCGTCAGTATCGATCGTCTGGCGGCGTATAAAGACGTTGATGTGCTCTGTTTTGATCAC
GACAACAGCAAAGACATGGATGCGCTAATGGCAACGCCGCTGTGGCAGGCCATGCCGTTT
GTCCGCGCCGGACGCTTTCAGCGCGTACCTGCAGTCTGGTTTTATGGTGCGACGCTCTCG
GCAATGCACTTTGTGCGCGTTCTGGATAACGCCATCGGAGGTAAAGCGTGA
Protein Properties
Pfam Domain Function:
Protein Residues:296
Protein Molecular Weight:32998
Protein Theoretical pI:6
PDB File:1K2V
Signaling Regions:
  • 1-30
Transmembrane Regions:
  • None
Protein Sequence:
>Iron(3+)-hydroxamate-binding protein fhuD
MSGLPLISRRRLLTAMALSPLLWQMNTAHAAAIDPNRIVALEWLPVELLLALGIVPYGVA
DTINYRLWVSEPPLPDSVIDVGLRTEPNLELLTEMKPSFMVWSAGYGPSPEMLARIAPGR
GFNFSDGKQPLAMARKSLTEMADLLNLQSAAETHLAQYEDFIRSMKPRFVKRGARPLLLT
TLIDPRHMLVFGPNSLFQEILDEYGIPNAWQGETNFWGSTAVSIDRLAAYKDVDVLCFDH
DNSKDMDALMATPLWQAMPFVRAGRFQRVPAVWFYGATLSAMHFVRVLDNAIGGKA
References
External Links:
ResourceLink
Uniprot ID:P07822
Uniprot Name:FHUD_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674358
PDB ID:1K2V
Ecogene ID:EG10305
Ecocyc:EG10305
ColiBase:b0152
Kegg Gene:b0152
EchoBASE ID:EB0301
CCDB:FHUD_ECOLI
BacMap:16128145
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Burkhardt, R., Braun, V. (1987). "Nucleotide sequence of the fhuC and fhuD genes involved in iron (III) hydroxamate transport: domains in FhuC homologous to ATP-binding proteins." Mol Gen Genet 209:49-55. Pubmed: 2823072
  • Clarke, T. E., Braun, V., Winkelmann, G., Tari, L. W., Vogel, H. J. (2002). "X-ray crystallographic structures of the Escherichia coli periplasmic protein FhuD bound to hydroxamate-type siderophores and the antibiotic albomycin." J Biol Chem 277:13966-13972. Pubmed: 11805094
  • Clarke, T. E., Ku, S. Y., Dougan, D. R., Vogel, H. J., Tari, L. W. (2000). "The structure of the ferric siderophore binding protein FhuD complexed with gallichrome." Nat Struct Biol 7:287-291. Pubmed: 10742172
  • Coulton, J. W., Mason, P., Allatt, D. D. (1987). "fhuC and fhuD genes for iron (III)-ferrichrome transport into Escherichia coli K-12." J Bacteriol 169:3844-3849. Pubmed: 3301821
  • Fujita, N., Mori, H., Yura, T., Ishihama, A. (1994). "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region." Nucleic Acids Res 22:1637-1639. Pubmed: 8202364
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Rohrback, M. R., Paul, S., Koster, W. (1995). "In vivo reconstitution of an active siderophore transport system by a binding protein derivative lacking a signal sequence." Mol Gen Genet 248:33-42. Pubmed: 7651325
  • Tullman-Ercek, D., DeLisa, M. P., Kawarasaki, Y., Iranpour, P., Ribnicky, B., Palmer, T., Georgiou, G. (2007). "Export pathway selectivity of Escherichia coli twin arginine translocation signal peptides." J Biol Chem 282:8309-8316. Pubmed: 17218314