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Q8FNZ7 (HIS4_COREF) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase

EC=5.3.1.16
Alternative name(s):
Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase
Gene names
Name:hisA
Ordered Locus Names:CE1996
OrganismCorynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395) [Complete proteome] [HAMAP]
Taxonomic identifier196164 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length246 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

1-(5-phospho-beta-D-ribosyl)-5-((5-phospho-beta-D-ribosylamino)methylideneamino)imidazole-4-carboxamide = 5-((5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino)-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide. HAMAP-Rule MF_01014

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9. HAMAP-Rule MF_01014

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01014.

Sequence similarities

Belongs to the HisA/HisF family.

Caution

Ala-129 is present instead of the conserved Asp which is expected to be an active site residue.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2462461-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase HAMAP-Rule MF_01014
PRO_0000142000

Sites

Active site101Proton acceptor By similarity

Secondary structure

............................................. 246
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8FNZ7 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: EF62454178C09B50

FASTA24626,624
        10         20         30         40         50         60 
MTFTILPAVD VVNGQAVRLD QGEAGTEKSY GTPLESALRW QEQGAEWLHF VDLDAAFNRG 

        70         80         90        100        110        120 
SNHELMAEIT RQLDIKVELT GGIRDDASLE RALATGATRV NIGTAALEKP EWIADVIRRH 

       130        140        150        160        170        180 
GEKIAVDIAV RLENGEWRTK GNGWVSDGGD LWEVLERLDS QGCSRFVVTD VSKDGTLTGP 

       190        200        210        220        230        240 
NVDLLRDVAA ATDAPIVASG GISTLEDVLG LAKYQDEGID SVIIGKALYE HRFTLAEALE 


AVEKLG 

« Hide

References

[1]"Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens."
Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.
Genome Res. 13:1572-1579(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000035 Genomic DNA. Translation: BAC18806.1.
RefSeqNP_738606.1. NC_004369.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4AXKX-ray2.25A/B1-246[»]
ProteinModelPortalQ8FNZ7.
SMRQ8FNZ7. Positions 5-241.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING196164.CE1996.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC18806; BAC18806; BAC18806.
GeneID1032056.
KEGGcef:CE1996.
PATRIC21490125. VBICorEff9312_1977.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000224614.
KOK01814.
OMATNIDSEG.
OrthoDBEOG6H1Q3W.

Enzyme and pathway databases

UniPathwayUPA00031; UER00009.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01014. HisA.
InterProIPR013785. Aldolase_TIM.
IPR006062. His_biosynth.
IPR010188. HisA_TrpF.
IPR023016. Isoase_HisA.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamPF00977. His_biosynth. 1 hit.
[Graphical view]
SUPFAMSSF51366. SSF51366. 1 hit.
TIGRFAMsTIGR01919. hisA-trpF. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHIS4_COREF
AccessionPrimary (citable) accession number: Q8FNZ7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2003
Last sequence update: March 1, 2003
Last modified: May 14, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways