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Protein

Histidinol-phosphate aminotransferase

Gene

hisC

Organism
Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152)
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 HisF (hisF), Imidazole glycerol phosphate synthase subunit HisH (hisH)
  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:BDI_0968
OrganismiParabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152)
Taxonomic identifieri435591 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesTannerellaceaeParabacteroides
Proteomesi
  • UP000000566 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000634891 – 345Histidinol-phosphate aminotransferaseAdd BLAST345

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei205N6-(pyridoxal phosphate)lysineUniRule annotation1

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi435591.BDI_0968.

Structurei

3D structure databases

ProteinModelPortaliA6LAM2.
SMRiA6LAM2.
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.
HOGENOMiHOG000288512.
KOiK00817.
OMAiTYGMYKV.
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
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.

A6LAM2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKDLKDLVRP NVWNLKPYSS ARDEFHGDAS VFLDANENPW NMPYNRYPDP
60 70 80 90 100
LQWKLKDRLA VLKGVDRSSI FLGNGSDEAI DLVIRAFCEP GLDSVVTISP
110 120 130 140 150
SYGMYEVAAN VNNVECRKVS LDENFDLDAE AVLESADEWT KVIFLCSPNN
160 170 180 190 200
PSGNSLDRGS IYKILKNYEG IVVIDEAYID FSAYPSFLKE LSGFPNLIVL
210 220 230 240 250
QTLSKAWGAA GIRLGMAFAS PEIIGVLNKI KYPYNVNQLT QEKALELLND
260 270 280 290 300
EATMKHQVNE ILTERNRLEK ILSEPPFSYQ VYPSDANFLL VNVAKADAMY
310 320 330 340
NGLVKKGIVV RNRSNVQKCR GCLRITIGTP KENDSLLNAM KNMKL
Length:345
Mass (Da):38,728
Last modified:July 24, 2007 - v1
Checksum:iF42CA52424812ECA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000140 Genomic DNA. Translation: ABR42736.1.
RefSeqiWP_005857193.1. NC_009615.1.

Genome annotation databases

EnsemblBacteriaiABR42736; ABR42736; BDI_0968.
GeneIDi5306122.
KEGGipdi:BDI_0968.

Similar proteinsi

Entry informationi

Entry nameiHIS8_PARD8
AccessioniPrimary (citable) accession number: A6LAM2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: July 24, 2007
Last modified: August 30, 2017
This is version 63 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