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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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 356356Histidinol-phosphate aminotransferasePRO_0000153360Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei214 – 2141N6-(pyridoxal phosphate)lysine

Proteomic databases

EPDiP06986.
PaxDbiP06986.

Interactioni

Subunit structurei

Homodimer.2 Publications

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

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

Structurei

Secondary structure

1
356
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 94Combined sources
Helixi12 – 165Combined sources
Turni27 – 293Combined sources
Beta strandi31 – 333Combined sources
Helixi61 – 7111Combined sources
Helixi75 – 773Combined sources
Beta strandi78 – 825Combined sources
Helixi83 – 9513Combined sources
Turni98 – 1003Combined sources
Beta strandi102 – 1054Combined sources
Beta strandi107 – 1093Combined sources
Helixi112 – 1209Combined sources
Beta strandi123 – 1264Combined sources
Helixi137 – 1415Combined sources
Beta strandi147 – 1559Combined sources
Turni157 – 1593Combined sources
Helixi165 – 17511Combined sources
Turni176 – 1783Combined sources
Beta strandi180 – 1845Combined sources
Helixi188 – 1903Combined sources
Helixi192 – 1943Combined sources
Helixi197 – 1993Combined sources
Turni200 – 2023Combined sources
Beta strandi206 – 2149Combined sources
Helixi219 – 2213Combined sources
Beta strandi224 – 2285Combined sources
Helixi230 – 23910Combined sources
Helixi247 – 25610Combined sources
Helixi259 – 28527Combined sources
Beta strandi289 – 2924Combined sources
Beta strandi296 – 3049Combined sources
Helixi307 – 31610Combined sources
Beta strandi333 – 3375Combined sources
Helixi341 – 35212Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 3-356.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06986.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CIH. Bacteria.
COG0079. LUCA.
HOGENOMiHOG000288512.
InParanoidiP06986.
KOiK00817.
OMAiYPSEANY.
OrthoDBiEOG651SWW.
PhylomeDBiP06986.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_01023. HisC_aminotrans_2.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti130 – 1301L → P (PubMed:3062174).Curated
Sequence conflicti130 – 1301L → P (PubMed:2999081).Curated
Sequence conflicti149 – 1491V → A (PubMed:3062174).Curated
Sequence conflicti149 – 1491V → A (PubMed:2999081).Curated

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
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. Positions 3-356.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

EPDiP06986.
PaxDbiP06986.

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.
OrthoDBiEOG651SWW.
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.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and function of the Salmonella typhimurium and Escherichia coli K-12 histidine operons."
    Carlomagno M.S., Chiariotti L., Alifano P., Nappo A.G., Bruni C.B.
    J. Mol. Biol. 203:585-606(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Cloning, structure, and expression of the Escherichia coli K-12 hisC gene."
    Grisolia V., Carlomagno M.S., Nappo A.G., Bruni C.B.
    J. Bacteriol. 164:1317-1323(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY.
    Strain: K12.
  3. "Nucleotide sequence of the Escherichia coli K12 histidine operon revisited."
    Jovanovic G., Kostic T., Jankovic M., Savic D.J.
    J. Mol. Biol. 239:433-435(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION.
    Strain: K12.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  6. "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.
  7. "Crystal structure of histidinol phosphate aminotransferase (HisC) from Escherichia coli, and its covalent complex with pyridoxal-5'-phosphate and L-histidinol phosphate."
    Sivaraman J., Li Y., Larocque R., Schrag J.D., Cygler M., Matte A.
    J. Mol. Biol. 311:761-776(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS), COFACTOR, SUBUNIT.
  8. "Structures of Escherichia coli histidinol-phosphate aminotransferase and its complexes with histidinol-phosphate and N-(5'-phosphopyridoxyl)-L-glutamate: double substrate recognition of the enzyme."
    Haruyama K., Nakai T., Miyahara I., Hirotsu K., Mizuguchi H., Hayashi H., Kagamiyama H.
    Biochemistry 40:4633-4644(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 5-351 IN COMPLEX WITH PYRIDOXAL 5'-PHOSPHATE; HISTIDINOL-PHOSPHATE AND N-(5'-PHOSPHOPYRIDOXYL)-L-GLUTAMATE, COFACTOR.

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: March 16, 2016
This is version 158 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.