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Protein

Histidinol-phosphate aminotransferase

Gene

hisC

Organism
Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
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 regulatory subunit (hisZ), ATP phosphoribosyltransferase (hisG)
  2. Phosphoribosyl-ATP pyrophosphatase (hisE)
  3. Phosphoribosyl-AMP cyclohydrolase (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. Imidazoleglycerol-phosphate dehydratase (hisB)
  7. Histidinol-phosphate aminotransferase (hisC)
  8. no protein annotated in this organism
  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

BioCyciLPLA220668:G137Z-2189-MONOMER.
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:lp_2551
OrganismiLactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
Taxonomic identifieri220668 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus
Proteomesi
  • UP000000432 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001533751 – 356Histidinol-phosphate aminotransferaseAdd BLAST356

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei222N6-(pyridoxal phosphate)lysineUniRule annotation1

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi220668.lp_2551.

Structurei

3D structure databases

ProteinModelPortaliQ88UE6.
SMRiQ88UE6.
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.
OMAiTYGMYKV.

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.
TIGRFAMsiTIGR01141. hisC. 1 hit.

Sequencei

Sequence statusi: Complete.

Q88UE6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKASIEQLEP YVPEKPLATL QAELGLTELV RLSANENPYG TSPKVATAVK
60 70 80 90 100
NWDFTQSNRY PDADAQELRQ AVAQQQGIDP NSIVFSVGLD EMIVMLSRTF
110 120 130 140 150
LATNDQVLVS APTFSEYGLH AEIEGGQLIS VPTLPNDHVN FEGLMKAITP
160 170 180 190 200
HVKMVWLCNP NNPTGTVESL AAIEAFVQQV PPETMVLIDE AYIDFTPGAA
210 220 230 240 250
QVTAMQLPAK YPNVVVMRTF SKAYGLANFR IGYAVFNTKY AATMQTIRLP
260 270 280 290 300
YNVNSLAQVA ALAAIDDPNF VKQTVQKNAT ERAKWMAFFD DQGVTYDQSG
310 320 330 340 350
ANFIFFKYPS ATQLADYLVH HGYLIRTGLR PGWLRLTVGT ANDNQQLQQL

IREFKA
Length:356
Mass (Da):39,431
Last modified:June 1, 2003 - v1
Checksum:i6CD0EDCE25860119
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL935263 Genomic DNA. Translation: CCC79707.1.
RefSeqiWP_011101825.1. NC_004567.2.
YP_004890221.1. NC_004567.2.

Genome annotation databases

EnsemblBacteriaiCCC79707; CCC79707; lp_2551.
GeneIDi1062746.
KEGGilpl:lp_2551.
PATRICifig|220668.9.peg.2143.

Similar proteinsi

Entry informationi

Entry nameiHIS8_LACPL
AccessioniPrimary (citable) accession number: Q88UE6
Secondary accession number(s): F9UR68
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 31, 2003
Last sequence update: June 1, 2003
Last modified: August 30, 2017
This is version 88 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