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Protein

Histidinol-phosphate aminotransferase

Gene

hisC

Organism
Paracoccus denitrificans (strain Pd 1222)
Status
Reviewed-Annotation score: Annotation score: 3 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 (Pden_1923)
  2. Phosphoribosyl-ATP pyrophosphatase (hisE)
  3. Phosphoribosyl-AMP cyclohydrolase (Pden_1336), 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), 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
Synonyms:hisH
Ordered Locus Names:Pden_1409
OrganismiParacoccus denitrificans (strain Pd 1222)
Taxonomic identifieri318586 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeParacoccus
Proteomesi
  • UP000000361 Componenti: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001534091 – 367Histidinol-phosphate aminotransferaseAdd BLAST367

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei221N6-(pyridoxal phosphate)lysineUniRule annotation1

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi318586.Pden_1409.

Structurei

3D structure databases

ProteinModelPortaliQ51687.
SMRiQ51687.
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.
TIGRFAMsiTIGR01141. hisC. 1 hit.

Sequencei

Sequence statusi: Complete.

Q51687-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQNQTTIAP QPGIMEISLY EGGASKVAGV ENVVKLSSNE NPFGPSDKAR
60 70 80 90 100
EAMIRAAHGL HRYPNTDHAG LRGAIGEVHG LDPDRIICGV GSDEIIHFLC
110 120 130 140 150
QAYAGPGTEV LFTEHGFLMY RISAHAAGAI PVQVAERDRV TDIDALIAGA
160 170 180 190 200
TPRTRLIFVA NPNNPTGTMV GLPELERLAR AVPQAILVVD AAYAEYVGDY
210 220 230 240 250
DGGAELATRL PNVFMTRTFS KIYGLGGLRV GWGYGPREIV DVLNRIRGPF
260 270 280 290 300
NLSNVALEGA EAAMRDREHI ARCQAENARM RAWLAEALAE KGVPSDTSCA
310 320 330 340 350
NFILARFADA ETAGACDEYL KTQGLIVRRV AGYGLPHCLR ITIGDEASCR
360
RVAHVIGQYM AERAESR
Length:367
Mass (Da):39,582
Last modified:March 6, 2007 - v2
Checksum:i49C86EA0501EB76B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti9A → R in CAA96498 (PubMed:9043133).Curated1
Sequence conflicti153Missing in CAA96498 (PubMed:9043133).Curated1
Sequence conflicti163N → K in CAA96498 (PubMed:9043133).Curated1
Sequence conflicti185 – 186AI → RIA in CAA96498 (PubMed:9043133).Curated2
Sequence conflicti205E → Q in CAA96498 (PubMed:9043133).Curated1
Sequence conflicti208 – 209TR → QA in CAA96498 (PubMed:9043133).Curated2
Sequence conflicti248G → A in CAA96498 (PubMed:9043133).Curated1
Sequence conflicti357 – 363GQYMAER → ASTWPSA in CAA96498 (PubMed:9043133).Curated7

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z71971 Genomic DNA. Translation: CAA96498.1.
CP000489 Genomic DNA. Translation: ABL69510.1.
RefSeqiWP_011747728.1. NC_008686.1.

Genome annotation databases

EnsemblBacteriaiABL69510; ABL69510; Pden_1409.
KEGGipde:Pden_1409.

Similar proteinsi

Entry informationi

Entry nameiHIS8_PARDP
AccessioniPrimary (citable) accession number: Q51687
Secondary accession number(s): A1B1W6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: March 6, 2007
Last modified: June 7, 2017
This is version 101 of the entry and version 2 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