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
Vibrio campbellii (strain ATCC BAA-1116 / BB120)
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 HisH (hisH), 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), 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:VIBHAR_01832
OrganismiVibrio campbellii (strain ATCC BAA-1116 / BB120)
Taxonomic identifieri338187 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
Proteomesi
  • UP000008152 Componenti: Chromosome I

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000635101 – 346Histidinol-phosphate aminotransferaseAdd BLAST346

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei209N6-(pyridoxal phosphate)lysineUniRule annotation1

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi338187.VIBHAR_01832.

Structurei

3D structure databases

ProteinModelPortaliA7MX17.
SMRiA7MX17.
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.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
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.

A7MX17-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKLARKQVQ QLTPYLSARR IGGTGDVWLN ANESPFNNEY KTDFARLNRY
60 70 80 90 100
SECQPKELIS AYAAYAGVKP EQTLTSRGAD EGIELLIRAF CEPGEDAILY
110 120 130 140 150
CPPTYGMYGI SAETIGVERK TVPLTSDWQL ELAGIEANLD NVKLVFVCSP
160 170 180 190 200
NNPTGNLVKR EDIVSLLEMT KDRAIVVMDE AYIDFCPEAS TVDLLAQYPN
210 220 230 240 250
LAILRTLSKA FALAGLRCGF TLANEELINV LLKVIAPYPV PVPVAEIATQ
260 270 280 290 300
ALSEAGLARA KFQVLDLNAN RAYLQVGLSM IPVLEVFEGW GNYLLVKFPD
310 320 330 340
GDGLFKAAWE TGIILRNSPI ENCVRISVGN RDECEKTLGF IRNYYA
Length:346
Mass (Da):38,261
Last modified:October 2, 2007 - v1
Checksum:iF749F886AA238831
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000789 Genomic DNA. Translation: ABU70801.1.
RefSeqiWP_012127626.1. NC_022269.1.

Genome annotation databases

EnsemblBacteriaiABU70801; ABU70801; VIBHAR_01832.
GeneIDi5553193.
KEGGivca:M892_04015.
vha:VIBHAR_01832.
PATRICifig|338187.25.peg.844.

Similar proteinsi

Entry informationi

Entry nameiHIS8_VIBCB
AccessioniPrimary (citable) accession number: A7MX17
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 2, 2007
Last modified: November 22, 2017
This is version 68 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

Documents

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