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Protein

Histidinol-phosphate aminotransferase

Gene

hisC

Organism
Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CIP 105152 / NBRC 16084 / F199)
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. Phosphoribosyl-ATP pyrophosphatase (hisE)
  3. Phosphoribosyl-AMP cyclohydrolase (Saro_2107)
  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), 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:Saro_0695
OrganismiNovosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CIP 105152 / NBRC 16084 / F199)
Taxonomic identifieri279238 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeNovosphingobium
Proteomesi
  • UP000009134 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003197811 – 372Histidinol-phosphate aminotransferaseAdd BLAST372

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei226N6-(pyridoxal phosphate)lysineUniRule annotation1

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi279238.Saro_0695.

Structurei

3D structure databases

ProteinModelPortaliQ2GAI1.
SMRiQ2GAI1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105CIH. Bacteria.
COG0079. LUCA.
HOGENOMiHOG000288510.
KOiK00817.
OMAiHGFLVYR.
OrthoDBiPOG091H05S1.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_01023. HisC_aminotrans_2. 1 hit.
InterProiView protein in InterPro
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.

Sequencei

Sequence statusi: Complete.

Q2GAI1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANAPQLPAS PQPKDWILGI HAYVPGKSTG KDGQVLTKLS ANENPLGTSA
60 70 80 90 100
AALEARAHAG DPARYPDPDS KDLRAAIGEV HGIDPSRIVM GTGSDELLNL
110 120 130 140 150
AAQAYAGPGD EVLYVRYGFS VYDIAARRCG AVPVVAPDAD YGTDVDALLA
160 170 180 190 200
CVTERTRVVF LANPNNPTGS WLPREEVARL HAGLRSDILL VLDGAYAEYL
210 220 230 240 250
DPANDDGALD LAVTACNVLV TRTFSKIYGL AGERIGWGTG HPAIVDMLNR
260 270 280 290 300
IRGPFNISLT GQAAGLAAVR DQAFVEASRR HNAHQRTRFV GKLEALGNHG
310 320 330 340 350
VRPLPSQANF VLILFEGKVT AEDVYLGLMD YGYITRWLPG QGLPQALRIT
360 370
IGTEAQMDEI ADAIRRMCEA AR
Length:372
Mass (Da):39,831
Last modified:March 21, 2006 - v1
Checksum:i4EDEC0211D5E269E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000248 Genomic DNA. Translation: ABD25142.1.
RefSeqiWP_011444356.1. NC_007794.1.

Genome annotation databases

EnsemblBacteriaiABD25142; ABD25142; Saro_0695.
KEGGinar:Saro_0695.

Similar proteinsi

Entry informationi

Entry nameiHIS8_NOVAD
AccessioniPrimary (citable) accession number: Q2GAI1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: March 21, 2006
Last modified: June 7, 2017
This is version 77 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, Reference proteome

Documents

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