Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase

Gene

hisA

Organism
Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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.UniRule annotation

Pathwayi: L-histidine biosynthesis

This protein is involved in step 4 of the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate.UniRule annotation
Proteins known to be involved in the 9 steps of the subpathway in this organism are:
  1. ATP phosphoribosyltransferase (hisG)
  2. Phosphoribosyl-ATP pyrophosphatase (hisE)
  3. Phosphoribosyl-AMP cyclohydrolase (hisI)
  4. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (hisA)
  5. Imidazole glycerol phosphate synthase subunit HisF (hisF), Imidazole glycerol phosphate synthase subunit HisH (hisH)
  6. Imidazoleglycerol-phosphate dehydratase (hisB)
  7. Histidinol-phosphate aminotransferase (hisC)
  8. no protein annotated in this organism
  9. Histidinol dehydrogenase (hisD)
This subpathway is part of the pathway L-histidine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate, the pathway L-histidine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei10Proton acceptorUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesis

Enzyme and pathway databases

UniPathwayiUPA00031; UER00009.

Names & Taxonomyi

Protein namesi
Recommended name:
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomeraseUniRule annotation (EC:5.3.1.16UniRule annotation)
Alternative name(s):
Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomeraseUniRule annotation
Gene namesi
Name:hisAUniRule annotation
Ordered Locus Names:CE1996
OrganismiCorynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
Taxonomic identifieri196164 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesCorynebacteriaceaeCorynebacterium
Proteomesi
  • UP000001409 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001420001 – 2461-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomeraseAdd BLAST246

Interactioni

Protein-protein interaction databases

STRINGi196164.HMPREF0290_2028.

Structurei

Secondary structure

1246
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 12Combined sources9
Beta strandi15 – 17Combined sources3
Helixi33 – 42Combined sources10
Beta strandi47 – 52Combined sources6
Helixi53 – 56Combined sources4
Helixi63 – 72Combined sources10
Beta strandi76 – 82Combined sources7
Helixi86 – 93Combined sources8
Turni94 – 96Combined sources3
Beta strandi98 – 102Combined sources5
Helixi105 – 108Combined sources4
Helixi110 – 120Combined sources11
Helixi121 – 123Combined sources3
Beta strandi124 – 133Combined sources10
Beta strandi136 – 139Combined sources4
Helixi151 – 160Combined sources10
Beta strandi166 – 170Combined sources5
Helixi173 – 175Combined sources3
Beta strandi176 – 178Combined sources3
Helixi182 – 191Combined sources10
Beta strandi196 – 200Combined sources5
Helixi205 – 212Combined sources8
Helixi213 – 217Combined sources5
Beta strandi219 – 225Combined sources7
Helixi226 – 229Combined sources4
Helixi235 – 246Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4AXKX-ray2.25A/B1-246[»]
ProteinModelPortaliQ8FNZ7.
SMRiQ8FNZ7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the HisA/HisF family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CJV. Bacteria.
COG0106. LUCA.
HOGENOMiHOG000224614.
KOiK01814.
OMAiEWLHLVD.
OrthoDBiPOG091H048O.

Family and domain databases

CDDicd04732. HisA. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01014. HisA. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR006062. His_biosynth.
IPR010188. HisA_TrpF.
IPR023016. Isoase_HisA.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamiPF00977. His_biosynth. 1 hit.
[Graphical view]
SUPFAMiSSF51366. SSF51366. 1 hit.
TIGRFAMsiTIGR01919. hisA-trpF. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8FNZ7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTFTILPAVD VVNGQAVRLD QGEAGTEKSY GTPLESALRW QEQGAEWLHF
60 70 80 90 100
VDLDAAFNRG SNHELMAEIT RQLDIKVELT GGIRDDASLE RALATGATRV
110 120 130 140 150
NIGTAALEKP EWIADVIRRH GEKIAVDIAV RLENGEWRTK GNGWVSDGGD
160 170 180 190 200
LWEVLERLDS QGCSRFVVTD VSKDGTLTGP NVDLLRDVAA ATDAPIVASG
210 220 230 240
GISTLEDVLG LAKYQDEGID SVIIGKALYE HRFTLAEALE AVEKLG
Length:246
Mass (Da):26,624
Last modified:March 1, 2003 - v1
Checksum:iEF62454178C09B50
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000035 Genomic DNA. Translation: BAC18806.1.
RefSeqiWP_006767994.1. NZ_GG700683.1.

Genome annotation databases

EnsemblBacteriaiBAC18806; BAC18806; BAC18806.
KEGGicef:CE1996.
PATRICi21490125. VBICorEff9312_1977.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000035 Genomic DNA. Translation: BAC18806.1.
RefSeqiWP_006767994.1. NZ_GG700683.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4AXKX-ray2.25A/B1-246[»]
ProteinModelPortaliQ8FNZ7.
SMRiQ8FNZ7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi196164.HMPREF0290_2028.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAC18806; BAC18806; BAC18806.
KEGGicef:CE1996.
PATRICi21490125. VBICorEff9312_1977.

Phylogenomic databases

eggNOGiENOG4105CJV. Bacteria.
COG0106. LUCA.
HOGENOMiHOG000224614.
KOiK01814.
OMAiEWLHLVD.
OrthoDBiPOG091H048O.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00009.

Family and domain databases

CDDicd04732. HisA. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01014. HisA. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR006062. His_biosynth.
IPR010188. HisA_TrpF.
IPR023016. Isoase_HisA.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamiPF00977. His_biosynth. 1 hit.
[Graphical view]
SUPFAMiSSF51366. SSF51366. 1 hit.
TIGRFAMsiTIGR01919. hisA-trpF. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiHIS4_COREF
AccessioniPrimary (citable) accession number: Q8FNZ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 6, 2003
Last sequence update: March 1, 2003
Last modified: November 2, 2016
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.