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Protein

Histidinol-phosphate aminotransferase 2

Gene

hisC2

Organism
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Status
Reviewed-Annotation score: Annotation score: 3 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 2 (hisH2), Imidazole glycerol phosphate synthase, cyclase subunit HisF (hisF), Imidazole glycerol phosphate synthase subunit HisH 1 (hisH1), Imidazoleglycerol-phosphate synthase, cyclase subunit HisF (lpg1194)
  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

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:lpg1998
OrganismiLegionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Taxonomic identifieri272624 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella
Proteomesi
  • UP000000609 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001533821 – 369Histidinol-phosphate aminotransferase 2Add BLAST369

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei231N6-(pyridoxal phosphate)lysineUniRule annotation1

Proteomic databases

PaxDbiQ5ZU10.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi272624.lpg1998.

Structurei

3D structure databases

ProteinModelPortaliQ5ZU10.
SMRiQ5ZU10.
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.

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.

Q5ZU10-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIDFQQLPH AGIRSLIPYV PGKSIEELAK EKGITDIIKL ASNENPLGCS
60 70 80 90 100
PLALSVIQTM SSHYIATYPS PWNHPLMSKL ASYLKVKPEQ LFLSNGSDYL
110 120 130 140 150
FNILLNCFAL HTDRHILTHD YAFSTYAIQA NSLQIPINSV PIGHNWEVNI
160 170 180 190 200
TDIVNACNQQ TGIIFIANPN NPTGVLIQQE EIKYLLEQIP KSTLLVLDEA
210 220 230 240 250
YYEFAASQLT VNSLDWLEEH PNLVVTRTFS KIYGMAGLRL GYAIANPSII
260 270 280 290 300
NILKRVQLPF IVNQVALAAA YAAIDDDDFI QSSLKMNNEG MLQLQAGFNE
310 320 330 340 350
LNIKYLPSSC NFLTFDCEED SMALYNYLLD NGIIVRPLHA YKMNNFIRVT
360
IGTKEQNSRF LTALKNFYL
Length:369
Mass (Da):41,489
Last modified:January 10, 2006 - v2
Checksum:i273B5EFEFE6AC97E
GO

Sequence cautioni

The sequence AAU28067 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017354 Genomic DNA. Translation: AAU28067.1. Different initiation.
RefSeqiYP_096014.1. NC_002942.5.

Genome annotation databases

EnsemblBacteriaiAAU28067; AAU28067; lpg1998.
GeneIDi19833564.
KEGGilpn:lpg1998.
PATRICifig|272624.6.peg.2091.

Similar proteinsi

Entry informationi

Entry nameiHIS82_LEGPH
AccessioniPrimary (citable) accession number: Q5ZU10
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: January 10, 2006
Last modified: June 7, 2017
This is version 94 of the entry and version 2 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