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Protein

Histidinol-phosphate aminotransferase 2

Gene

hisC2

Organism
Haemophilus influenzae (strain 86-028NP)
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 2 (hisC2), Histidinol-phosphate aminotransferase 1 (hisC1)
  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

BioCyciHINF281310:GJ89-1246-MONOMER.
UniPathwayiUPA00031; UER00012.

Names & Taxonomyi

Protein namesi
Recommended name:
Histidinol-phosphate aminotransferase 2UniRule annotation (EC:2.6.1.9UniRule annotation)
Alternative name(s):
Imidazole acetol-phosphate transaminase 2UniRule annotation
Gene namesi
Name:hisC2UniRule annotation
Ordered Locus Names:NTHI1334
OrganismiHaemophilus influenzae (strain 86-028NP)
Taxonomic identifieri281310 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
Proteomesi
  • UP000002525 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001533711 – 366Histidinol-phosphate aminotransferase 2Add BLAST366

Amino acid modifications

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

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ4QLD1.
SMRiQ4QLD1.
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.
OMAiPTFDGYP.
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
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.

Q4QLD1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQYINIANRG VKSLSPYQAG KPIEELEREI GISNIVKLAS NENPFGFPES
60 70 80 90 100
AKKAIFEQLD KLTRYPDANG FELKQTIAKK FGVQPNQITL GNGSNDLLEL
110 120 130 140 150
FAHTFATEGD EIIYSQYAFI VYPLVTKAIN AIAKEIPAKN WGHDLQGFLT
160 170 180 190 200
ALSDKTKLIY IANPNNPTGN FLTSQEIEDF LAKVPENVIV VLDEAYTEFT
210 220 230 240 250
RSEERVDSFS LLKKYSNLII SRTLSKAYGL AGLRIGYAVS NPEIADLLNR
260 270 280 290 300
VRQPFNCNSL ALTAAVAVMN DDEFIEKVAE NNRIEMRRYE DFCQKNQLDY
310 320 330 340 350
IPSKGNFITI DFKQPAAPIY DALLREGVIV RPIAGYGMPN HLRISIGLPE
360
ENDKFFTALS KVLKFA
Length:366
Mass (Da):41,035
Last modified:July 19, 2005 - v1
Checksum:iF8111B502A86EE29
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000057 Genomic DNA. Translation: AAX88166.1.
RefSeqiWP_011272420.1. NC_007146.2.

Genome annotation databases

EnsemblBacteriaiAAX88166; AAX88166; NTHI1334.
KEGGihit:NTHI1334.

Similar proteinsi

Entry informationi

Entry nameiHIS82_HAEI8
AccessioniPrimary (citable) accession number: Q4QLD1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: July 19, 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

Documents

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