Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Histidinol-phosphate aminotransferase

Gene

hisC

Organism
Campylobacter jejuni (strain RM1221)
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. no protein annotated in this organism
  3. no protein annotated in this organism
  4. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (hisA)
  5. Imidazole glycerol phosphate synthase subunit HisH 1 (hisH1), Imidazole glycerol phosphate synthase subunit HisH 2 (hisH2), Imidazole glycerol phosphate synthase subunit HisF (hisF)
  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:CJE0362
OrganismiCampylobacter jejuni (strain RM1221)
Taxonomic identifieri195099 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001533411 – 364Histidinol-phosphate aminotransferaseAdd BLAST364

Amino acid modifications

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

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ5HWF4.
SMRiQ5HWF4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000288510.
KOiK00817.
OMAiHGFLVYR.

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.

Q5HWF4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKFNEFLNHL SNYEPGKDIE VIAKEYGVKE VIKLASNENP FGTPPKAIEC
60 70 80 90 100
LRQNANKAHL YPDDSMIELK STLAQKYKVQ NENIIIGAGS DQVIEFAIHA
110 120 130 140 150
KLNSKNAFLQ AGVTFAMYEI YAKQCGAKCY KTQSITHDLN EFKKLYEAHK
160 170 180 190 200
DEIKLIFLCL PNNPLGECLD ASEVTKFIKG VDEDCLVVID AAYNEFASFK
210 220 230 240 250
DSKKHLEPCE LIKEFDNVLY LGTFSKLYGL GGLRIGYGIA NANIISAFYK
260 270 280 290 300
LRAPFNVSNL ALKAAVAAIN DDEFAKKTLE NNFSQMELYK EFAKKHNIKI
310 320 330 340 350
IDSYTNFITY FFNEKNSTDL SEKLLKKGII IRNLKSYGLN AIRITIGTSY
360
ENEKFFTEFD KILR
Length:364
Mass (Da):41,322
Last modified:February 15, 2005 - v1
Checksum:i007CB8EE53A2F040
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000025 Genomic DNA. Translation: AAW34951.1.
RefSeqiWP_002867750.1. NC_003912.7.

Genome annotation databases

EnsemblBacteriaiAAW34951; AAW34951; CJE0362.
KEGGicjr:CJE0362.

Similar proteinsi

Entry informationi

Entry nameiHIS8_CAMJR
AccessioniPrimary (citable) accession number: Q5HWF4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: February 15, 2005
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

Documents

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