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Protein

Histidinol-phosphate aminotransferase

Gene

hisC

Organism
Chelativorans sp. (strain BNC1)
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), 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:Meso_3084
OrganismiChelativorans sp. (strain BNC1)
Taxonomic identifieri266779 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesPhyllobacteriaceaeChelativorans
Proteomesi
  • UP000001820 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003197731 – 366Histidinol-phosphate aminotransferaseAdd BLAST366

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei223N6-(pyridoxal phosphate)lysineUniRule annotation1

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi266779.Meso_3084.

Structurei

3D structure databases

ProteinModelPortaliQ11DR9.
SMRiQ11DR9.
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.

Q11DR9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTALDHPQPR PGIKNIAAYV PGRESAPGVE KIWKLSSNET PLGPSPAALE
60 70 80 90 100
AVREASQHLE IYPDGSASKL RDAIAKAHGL NPANILCSNG SDELLALLAQ
110 120 130 140 150
TYLMPGDEGI YTEHGFLVYR IQILAAGATP VVAREKDERA DVDAILAAVT
160 170 180 190 200
ERTKIVFLAN PNNPTGTYLP MEEVKRLRSG LPRKVLLVLD AAYAEYVRRN
210 220 230 240 250
DYEAGVELVS SNDNVVMTRT FSKIHGLAGL RIGWMYAPIH VVDAVNRVRG
260 270 280 290 300
PFNVNAIAIE AGTAATHDKA HVERAVEHNE TWRTWLAQEL EKLGLRVTPS
310 320 330 340 350
VANFLLIHFP ENGSKTAEEA DAFLTARGYI LRRVTGYGFP HALRLTVGTE
360
EANRGVIAAL AEFLER
Length:366
Mass (Da):39,980
Last modified:August 22, 2006 - v1
Checksum:iC96FF6D860E6B094
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000390 Genomic DNA. Translation: ABG64456.1.
RefSeqiWP_011582397.1. NC_008254.1.

Genome annotation databases

EnsemblBacteriaiABG64456; ABG64456; Meso_3084.
KEGGimes:Meso_3084.

Similar proteinsi

Entry informationi

Entry nameiHIS8_CHESB
AccessioniPrimary (citable) accession number: Q11DR9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: August 22, 2006
Last modified: June 7, 2017
This is version 75 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