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Protein

Histidinol-phosphate aminotransferase

Gene

hisC

Organism
Escherichia coli (strain SMS-3-5 / SECEC)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

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

Cofactori

pyridoxal 5'-phosphateUniRule annotation

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.UniRule annotation
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

Keywordsi

Molecular functionAminotransferase, Transferase
Biological processAmino-acid biosynthesis, Histidine biosynthesis
LigandPyridoxal phosphate

Enzyme and pathway databases

UniPathwayiUPA00031; UER00012.

Names & Taxonomyi

Protein namesi
Recommended name:
Histidinol-phosphate aminotransferaseUniRule annotation (EC:2.6.1.9UniRule annotation)
Alternative name(s):
Imidazole acetol-phosphate transaminaseUniRule annotation
Gene namesi
Name:hisCUniRule annotation
Ordered Locus Names:EcSMS35_1039
OrganismiEscherichia coli (strain SMS-3-5 / SECEC)
Taxonomic identifieri439855 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000007011 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10001353981 – 356Histidinol-phosphate aminotransferaseAdd BLAST356

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei214N6-(pyridoxal phosphate)lysineUniRule annotation1

Proteomic databases

PRIDEiB1LP20.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliB1LP20.
SMRiB1LP20.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000288512.
KOiK00817.
OMAiTYGMYKV.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPiMF_01023. HisC_aminotrans_2. 1 hit.
InterProiView protein in InterPro
IPR001917. 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_sub2.
PfamiView protein in Pfam
PF00155. Aminotran_1_2. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01141. hisC. 1 hit.
PROSITEiView protein in PROSITE
PS00599. AA_TRANSFER_CLASS_2. 1 hit.

Sequencei

Sequence statusi: Complete.

B1LP20-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTVTITDLA RENVRNLTPY QSARRLGGNG DVWLNANEYP TAVEFQLTQQ
60 70 80 90 100
TLNRYPECQP KAVIENYAQY AGVKAEQVLV SRGADEGIEL LIRAFCEPGK
110 120 130 140 150
DAILYCPPTY GMYSVSAETI GVECRTVPTL KNWQLDLQGI 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 QIIAEREYLM AALKEIPCVE QVFDSETNYI
310 320 330 340 350
LARFKASSAV FKSLWDQGII LRDQNKQPSL SGCLRITVGT REESQRVIDA

LRAEQV
Length:356
Mass (Da):39,365
Last modified:April 29, 2008 - v1
Checksum:i50EFE08542448B23
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000970 Genomic DNA. Translation: ACB19219.1.
RefSeqiWP_000108926.1. NC_010498.1.

Genome annotation databases

EnsemblBacteriaiACB19219; ACB19219; EcSMS35_1039.
KEGGiecm:EcSMS35_1039.

Similar proteinsi

Entry informationi

Entry nameiHIS8_ECOSM
AccessioniPrimary (citable) accession number: B1LP20
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 29, 2008
Last modified: June 7, 2017
This is version 66 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families