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Protein

Iron-binding protein IscA

Gene

iscA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Is able to transfer iron-sulfur clusters to apo-ferredoxin. Multiple cycles of [2Fe2S] cluster formation and transfer are observed, suggesting that IscA acts catalytically. Recruits intracellular free iron so as to provide iron for the assembly of transient iron-sulfur cluster in IscU in the presence of IscS, L-cysteine and the thioredoxin reductase system TrxA/TrxB.

Cofactori

Fe cationNote: Binds 2 iron ions per dimer. The dimer may bind additional iron ions.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi35 – 351IronCurated
Metal bindingi99 – 991IronCurated
Metal bindingi101 – 1011IronCurated

GO - Molecular functioni

  • 2 iron, 2 sulfur cluster binding Source: UniProtKB
  • 4 iron, 4 sulfur cluster binding Source: GO_Central
  • ferrous iron binding Source: EcoCyc
  • iron chaperone activity Source: EcoCyc
  • structural molecule activity Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG12132-MONOMER.
ECOL316407:JW2512-MONOMER.
MetaCyc:EG12132-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Iron-binding protein IscA
Alternative name(s):
Iron-sulfur cluster assembly protein
Gene namesi
Name:iscA
Synonyms:yfhF
Ordered Locus Names:b2528, JW2512
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12132. iscA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi35 – 351C → S: Decrease of iron binding activity. 1 Publication
Mutagenesisi99 – 991C → S: Loss of iron binding activity. 1 Publication
Mutagenesisi101 – 1011C → S: Loss of iron binding activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 107107Iron-binding protein IscAPRO_0000076997Add
BLAST

Proteomic databases

EPDiP0AAC8.
PaxDbiP0AAC8.
PRIDEiP0AAC8.

Expressioni

Inductioni

Repressed by IscR.

Interactioni

Subunit structurei

Homodimer; may form tetramers and higher multimers.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
fdxP0A9R44EBI-767026,EBI-767037

Protein-protein interaction databases

BioGridi4260603. 23 interactions.
DIPiDIP-35854N.
IntActiP0AAC8. 5 interactions.
STRINGi511145.b2528.

Structurei

Secondary structure

1
107
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 2014Combined sources
Beta strandi24 – 329Combined sources
Beta strandi34 – 363Combined sources
Beta strandi38 – 4710Combined sources
Beta strandi52 – 576Combined sources
Beta strandi60 – 656Combined sources
Helixi66 – 683Combined sources
Helixi69 – 724Combined sources
Beta strandi76 – 827Combined sources
Beta strandi85 – 917Combined sources
Beta strandi93 – 953Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1R94X-ray2.30A/B1-105[»]
1R95X-ray2.65A/B1-105[»]
1S98X-ray2.30A/B1-107[»]
ProteinModelPortaliP0AAC8.
SMRiP0AAC8. Positions 1-97.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AAC8.

Family & Domainsi

Sequence similaritiesi

Belongs to the HesB/IscA family.Curated

Phylogenomic databases

eggNOGiENOG4108Z4V. Bacteria.
COG0316. LUCA.
HOGENOMiHOG000228314.
InParanoidiP0AAC8.
KOiK13628.
OMAiLAYSVDY.
OrthoDBiEOG6VXF8J.
PhylomeDBiP0AAC8.

Family and domain databases

Gene3Di2.60.300.12. 1 hit.
HAMAPiMF_01429. Fe_S_insert_IscA.
InterProiIPR000361. FeS_biogenesis.
IPR016092. FeS_cluster_insertion.
IPR017870. FeS_cluster_insertion_CS.
IPR031108. ISCA-like.
IPR011302. IscA_proteobacteria.
[Graphical view]
PANTHERiPTHR10072:SF48. PTHR10072:SF48. 1 hit.
PfamiPF01521. Fe-S_biosyn. 1 hit.
[Graphical view]
SUPFAMiSSF89360. SSF89360. 1 hit.
TIGRFAMsiTIGR02011. IscA. 1 hit.
TIGR00049. TIGR00049. 1 hit.
PROSITEiPS01152. HESB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0AAC8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSITLSDSAA ARVNTFLANR GKGFGLRLGV RTSGCSGMAY VLEFVDEPTP
60 70 80 90 100
EDIVFEDKGV KVVVDGKSLQ FLDGTQLDFV KEGLNEGFKF TNPNVKDECG

CGESFHV
Length:107
Mass (Da):11,556
Last modified:September 13, 2005 - v1
Checksum:iCBA945AD547E77DD
GO

Sequence cautioni

The sequence U01827 differs from that shown. Reason: Frameshift at several positions. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U01827 Unassigned DNA. No translation available.
U00096 Genomic DNA. Translation: AAC75581.1.
AP009048 Genomic DNA. Translation: BAA16422.1.
PIRiG65029.
RefSeqiNP_417023.1. NC_000913.3.
WP_000028953.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75581; AAC75581; b2528.
BAA16422; BAA16422; BAA16422.
GeneIDi946999.
KEGGiecj:JW2512.
eco:b2528.
PATRICi32120453. VBIEscCol129921_2629.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U01827 Unassigned DNA. No translation available.
U00096 Genomic DNA. Translation: AAC75581.1.
AP009048 Genomic DNA. Translation: BAA16422.1.
PIRiG65029.
RefSeqiNP_417023.1. NC_000913.3.
WP_000028953.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1R94X-ray2.30A/B1-105[»]
1R95X-ray2.65A/B1-105[»]
1S98X-ray2.30A/B1-107[»]
ProteinModelPortaliP0AAC8.
SMRiP0AAC8. Positions 1-97.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260603. 23 interactions.
DIPiDIP-35854N.
IntActiP0AAC8. 5 interactions.
STRINGi511145.b2528.

Proteomic databases

EPDiP0AAC8.
PaxDbiP0AAC8.
PRIDEiP0AAC8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75581; AAC75581; b2528.
BAA16422; BAA16422; BAA16422.
GeneIDi946999.
KEGGiecj:JW2512.
eco:b2528.
PATRICi32120453. VBIEscCol129921_2629.

Organism-specific databases

EchoBASEiEB2053.
EcoGeneiEG12132. iscA.

Phylogenomic databases

eggNOGiENOG4108Z4V. Bacteria.
COG0316. LUCA.
HOGENOMiHOG000228314.
InParanoidiP0AAC8.
KOiK13628.
OMAiLAYSVDY.
OrthoDBiEOG6VXF8J.
PhylomeDBiP0AAC8.

Enzyme and pathway databases

BioCyciEcoCyc:EG12132-MONOMER.
ECOL316407:JW2512-MONOMER.
MetaCyc:EG12132-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0AAC8.
PROiP0AAC8.

Family and domain databases

Gene3Di2.60.300.12. 1 hit.
HAMAPiMF_01429. Fe_S_insert_IscA.
InterProiIPR000361. FeS_biogenesis.
IPR016092. FeS_cluster_insertion.
IPR017870. FeS_cluster_insertion_CS.
IPR031108. ISCA-like.
IPR011302. IscA_proteobacteria.
[Graphical view]
PANTHERiPTHR10072:SF48. PTHR10072:SF48. 1 hit.
PfamiPF01521. Fe-S_biosyn. 1 hit.
[Graphical view]
SUPFAMiSSF89360. SSF89360. 1 hit.
TIGRFAMsiTIGR02011. IscA. 1 hit.
TIGR00049. TIGR00049. 1 hit.
PROSITEiPS01152. HESB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mutations in a gene encoding a new Hsp70 suppress rapid DNA inversion and bgl activation, but not proU derepression, in hns-1 mutant Escherichia coli."
    Kawula T.H., Lelivelt M.J.
    J. Bacteriol. 176:610-619(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
    Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
    , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
    DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite chromatography."
    Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.
    Electrophoresis 20:2181-2195(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: B / BL21.
  6. "Iron-sulfur cluster assembly: characterization of IscA and evidence for a specific and functional complex with ferredoxin."
    Ollagnier-de-Choudens S., Mattioli T., Takahashi Y., Fontecave M.
    J. Biol. Chem. 276:22604-22607(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION AS AN IRON-SULFUR CLUSTER ASSEMBLY PROTEIN.
  7. "Characterization of iron binding in IscA, an ancient iron-sulphur cluster assembly protein."
    Ding H., Clark R.J.
    Biochem. J. 379:433-440(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION AS AN IRON-BINDING PROTEIN.
  8. "IscA mediates iron delivery for assembly of iron-sulfur clusters in IscU under the limited accessible free iron conditions."
    Ding H., Clark R.J., Ding B.
    J. Biol. Chem. 279:37499-37504(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CYS-35; CYS-99 AND CYS-101.
  9. "Multiple turnover transfer of [2Fe2S] clusters by the iron-sulfur cluster assembly scaffold proteins IscU and IscA."
    Bonomi F., Iametti S., Ta D., Vickery L.E.
    J. Biol. Chem. 280:29513-29518(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TRANSFER OF IRON-SULFUR CLUSTERS.
  10. "Thioredoxin reductase system mediates iron binding in IscA and iron delivery for the iron-sulfur cluster assembly in IscU."
    Ding H., Harrison K., Lu J.
    J. Biol. Chem. 280:30432-30437(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ROLE OF THE THIOREDOXIN REDUCTASE SYSTEM.
  11. "Crystal structure of the ancient, Fe-S scaffold IscA reveals a novel protein fold."
    Bilder P.W., Ding H., Newcomer M.E.
    Biochemistry 43:133-139(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-105, SUBUNIT.
  12. "Crystal structure of IscA, an iron-sulfur cluster assembly protein from Escherichia coli."
    Cupp-Vickery J.R., Silberg J.J., Ta D.T., Vickery L.E.
    J. Mol. Biol. 338:127-137(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), SUBUNIT.

Entry informationi

Entry nameiISCA_ECOLI
AccessioniPrimary (citable) accession number: P0AAC8
Secondary accession number(s): P36539, P77691
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: September 13, 2005
Last modified: March 16, 2016
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

2 iron atoms may bind between dimers.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.