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Protein

Histidinol-phosphate aminotransferase

Gene

hisC

Organism
Vibrio fischeri (strain ATCC 700601 / ES114)
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)
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:VF_1014
OrganismiVibrio fischeri (strain ATCC 700601 / ES114)
Taxonomic identifieri312309 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeAliivibrio
Proteomesi
  • UP000000537 Componenti: Chromosome I

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001534751 – 346Histidinol-phosphate aminotransferaseAdd BLAST346

Amino acid modifications

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

Proteomic databases

PRIDEiQ5E637.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi312309.VF_1014.

Structurei

3D structure databases

ProteinModelPortaliQ5E637.
SMRiQ5E637.
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.
OrthoDBiPOG091H05S1.

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.

Q5E637-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKLARKQVQ ALTPYLSARR IGGSGDVWLN ANESPFDNEY QFNFARLNRY
60 70 80 90 100
SECQPPELIN AYAAYAKVKP EQVLTSRGAD EGIELLVRAF CEPNQDAILY
110 120 130 140 150
CPPTYGMYSI SAETIGVETK TVPLTSNWQL DLPAIEASLE NVKVVFVCSP
160 170 180 190 200
NNPTGNIVDR KDILSLLEMT KDRAIVVMDE AYIDFCMEKS TVDLLVDYPH
210 220 230 240 250
LAILRTLSKA FALAGLRCGF TLANEELINV LLKVIAPYPV PVPVAEIATQ
260 270 280 290 300
ALSEAGLARM KYQMLDLSAN RAYLQAGLMV LPGVTVFEGW GNYLLVKFPD
310 320 330 340
GDSVFKAAWD HGIILRNSPI ENCVRISVGN REECEKTLGF IRNQLI
Length:346
Mass (Da):38,435
Last modified:March 15, 2005 - v1
Checksum:iADDCF50AB9018C40
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000020 Genomic DNA. Translation: AAW85509.1.
RefSeqiWP_011261647.1. NC_006840.2.
YP_204397.1. NC_006840.2.

Genome annotation databases

EnsemblBacteriaiAAW85509; AAW85509; VF_1014.
GeneIDi3277156.
KEGGivfi:VF_1014.
PATRICifig|312309.11.peg.1014.

Similar proteinsi

Entry informationi

Entry nameiHIS8_VIBF1
AccessioniPrimary (citable) accession number: Q5E637
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: March 15, 2005
Last modified: June 7, 2017
This is version 73 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