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Protein

Histidinol-phosphate aminotransferase

Gene

hisC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

L-histidinol phosphate + 2-oxoglutarate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate.1 Publication

Cofactori

pyridoxal 5'-phosphate2 Publications

Pathwayi: L-histidine biosynthesis

This protein is involved in step 7 of the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate.1 Publication
Proteins known to be involved in the 9 steps of the subpathway in this organism are:
  1. ATP phosphoribosyltransferase (hisG)
  2. Histidine biosynthesis bifunctional protein HisIE (hisI)
  3. Histidine biosynthesis bifunctional protein HisIE (hisI)
  4. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (hisA)
  5. Imidazole glycerol phosphate synthase subunit HisH (hisH), Imidazole glycerol phosphate synthase subunit HisF (hisF)
  6. Histidine biosynthesis bifunctional protein HisB (hisB)
  7. Histidinol-phosphate aminotransferase (hisC)
  8. Histidine biosynthesis bifunctional protein HisB (hisB)
  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.

GO - Molecular functioni

GO - Biological processi

  • histidine biosynthetic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciEcoCyc:HISTPHOSTRANS-MONOMER.
ECOL316407:JW2003-MONOMER.
MetaCyc:HISTPHOSTRANS-MONOMER.
BRENDAi2.6.1.9. 2026.
UniPathwayiUPA00031; UER00012.

Names & Taxonomyi

Protein namesi
Recommended name:
Histidinol-phosphate aminotransferase (EC:2.6.1.9)
Alternative name(s):
Imidazole acetol-phosphate transaminase
Short name:
HPAT
Short name:
HspAT
Gene namesi
Name:hisC
Ordered Locus Names:b2021, JW2003
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10446. hisC.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001533601 – 356Histidinol-phosphate aminotransferaseAdd BLAST356

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei214N6-(pyridoxal phosphate)lysine1

Proteomic databases

EPDiP06986.
PaxDbiP06986.
PRIDEiP06986.

Interactioni

Subunit structurei

Homodimer.2 Publications

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4260404. 14 interactors.
DIPiDIP-9902N.
IntActiP06986. 5 interactors.
MINTiMINT-1322565.
STRINGi511145.b2021.

Structurei

Secondary structure

1356
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 9Combined sources4
Helixi12 – 16Combined sources5
Turni27 – 29Combined sources3
Beta strandi31 – 33Combined sources3
Helixi61 – 71Combined sources11
Helixi75 – 77Combined sources3
Beta strandi78 – 82Combined sources5
Helixi83 – 95Combined sources13
Turni98 – 100Combined sources3
Beta strandi102 – 105Combined sources4
Beta strandi107 – 109Combined sources3
Helixi112 – 120Combined sources9
Beta strandi123 – 126Combined sources4
Helixi137 – 141Combined sources5
Beta strandi147 – 155Combined sources9
Turni157 – 159Combined sources3
Helixi165 – 175Combined sources11
Turni176 – 178Combined sources3
Beta strandi180 – 184Combined sources5
Helixi188 – 190Combined sources3
Helixi192 – 194Combined sources3
Helixi197 – 199Combined sources3
Turni200 – 202Combined sources3
Beta strandi206 – 214Combined sources9
Helixi219 – 221Combined sources3
Beta strandi224 – 228Combined sources5
Helixi230 – 239Combined sources10
Helixi247 – 256Combined sources10
Helixi259 – 285Combined sources27
Beta strandi289 – 292Combined sources4
Beta strandi296 – 304Combined sources9
Helixi307 – 316Combined sources10
Beta strandi333 – 337Combined sources5
Helixi341 – 352Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FG3X-ray2.20A1-356[»]
1FG7X-ray1.50A1-356[»]
1GEWX-ray2.00A1-356[»]
1GEXX-ray2.20A1-356[»]
1GEYX-ray2.30A1-356[»]
1IJIX-ray2.20A1-356[»]
ProteinModelPortaliP06986.
SMRiP06986.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06986.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CIH. Bacteria.
COG0079. LUCA.
HOGENOMiHOG000288512.
InParanoidiP06986.
KOiK00817.
OMAiYPSEANY.
PhylomeDBiP06986.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_01023. HisC_aminotrans_2. 1 hit.
InterProiIPR001917. Aminotrans_II_pyridoxalP_BS.
IPR004839. Aminotransferase_I/II.
IPR005861. HisP_aminotrans.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01141. hisC. 1 hit.
PROSITEiPS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P06986-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTVTITDLA RENVRNLTPY QSARRLGGNG DVWLNANEYP TAVEFQLTQQ
60 70 80 90 100
TLNRYPECQP KAVIENYAQY AGVKPEQVLV SRGADEGIEL LIRAFCEPGK
110 120 130 140 150
DAILYCPPTY GMYSVSAETI GVECRTVPTL DNWQLDLQGI SDKLDGVKVV
160 170 180 190 200
YVCSPNNPTG QLINPQDFRT LLELTRGKAI VVADEAYIEF CPQASLAGWL
210 220 230 240 250
AEYPHLAILR TLSKAFALAG LRCGFTLANE EVINLLMKVI APYPLSTPVA
260 270 280 290 300
DIAAQALSPQ GIVAMRERVA QIIAEREYLI AALKEIPCVE QVFDSETNYI
310 320 330 340 350
LARFKASSAV FKSLWDQGII LRDQNKQPSL SGCLRITVGT REESQRVIDA

LRAEQV
Length:356
Mass (Da):39,360
Last modified:February 1, 1995 - v2
Checksum:i056CBB3CF894083F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti130L → P (PubMed:3062174).Curated1
Sequence conflicti130L → P (PubMed:2999081).Curated1
Sequence conflicti149V → A (PubMed:3062174).Curated1
Sequence conflicti149V → A (PubMed:2999081).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03416 Genomic DNA. Translation: CAA27150.1.
X13462 Genomic DNA. Translation: CAA31813.1.
U02071 Unassigned DNA. Translation: AAA19743.1.
U00096 Genomic DNA. Translation: AAC75082.1.
AP009048 Genomic DNA. Translation: BAA15852.1.
PIRiD64967. XNECHC.
RefSeqiNP_416525.1. NC_000913.3.
WP_000108941.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75082; AAC75082; b2021.
BAA15852; BAA15852; BAA15852.
GeneIDi946551.
KEGGiecj:JW2003.
eco:b2021.
PATRICi32119377. VBIEscCol129921_2098.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03416 Genomic DNA. Translation: CAA27150.1.
X13462 Genomic DNA. Translation: CAA31813.1.
U02071 Unassigned DNA. Translation: AAA19743.1.
U00096 Genomic DNA. Translation: AAC75082.1.
AP009048 Genomic DNA. Translation: BAA15852.1.
PIRiD64967. XNECHC.
RefSeqiNP_416525.1. NC_000913.3.
WP_000108941.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FG3X-ray2.20A1-356[»]
1FG7X-ray1.50A1-356[»]
1GEWX-ray2.00A1-356[»]
1GEXX-ray2.20A1-356[»]
1GEYX-ray2.30A1-356[»]
1IJIX-ray2.20A1-356[»]
ProteinModelPortaliP06986.
SMRiP06986.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260404. 14 interactors.
DIPiDIP-9902N.
IntActiP06986. 5 interactors.
MINTiMINT-1322565.
STRINGi511145.b2021.

Proteomic databases

EPDiP06986.
PaxDbiP06986.
PRIDEiP06986.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75082; AAC75082; b2021.
BAA15852; BAA15852; BAA15852.
GeneIDi946551.
KEGGiecj:JW2003.
eco:b2021.
PATRICi32119377. VBIEscCol129921_2098.

Organism-specific databases

EchoBASEiEB0441.
EcoGeneiEG10446. hisC.

Phylogenomic databases

eggNOGiENOG4105CIH. Bacteria.
COG0079. LUCA.
HOGENOMiHOG000288512.
InParanoidiP06986.
KOiK00817.
OMAiYPSEANY.
PhylomeDBiP06986.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00012.
BioCyciEcoCyc:HISTPHOSTRANS-MONOMER.
ECOL316407:JW2003-MONOMER.
MetaCyc:HISTPHOSTRANS-MONOMER.
BRENDAi2.6.1.9. 2026.

Miscellaneous databases

EvolutionaryTraceiP06986.
PROiP06986.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_01023. HisC_aminotrans_2. 1 hit.
InterProiIPR001917. Aminotrans_II_pyridoxalP_BS.
IPR004839. Aminotransferase_I/II.
IPR005861. HisP_aminotrans.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01141. hisC. 1 hit.
PROSITEiPS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHIS8_ECOLI
AccessioniPrimary (citable) accession number: P06986
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: February 1, 1995
Last modified: November 2, 2016
This is version 161 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.