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Protein

Histidinol-phosphate aminotransferase 2

Gene

hisC2

Organism
Legionella pneumophila (strain Paris)
Status
Reviewed-Annotation score: -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. no protein annotated in this organism
  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)
  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

UniPathwayi
UPA00031;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:lpp1979
OrganismiLegionella pneumophila (strain Paris)
Taxonomic identifieri297246 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella

Organism-specific databases

LegioListilpp1979

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001533801 – 369Histidinol-phosphate aminotransferase 2Add BLAST369

Amino acid modifications

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

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ5X3Q5
SMRiQ5X3Q5
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CIH Bacteria
COG0079 LUCA
HOGENOMiHOG000288510
KOiK00817
OMAiPTFDGYP
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
IPR004839 Aminotransferase_I/II
IPR005861 HisP_aminotrans
IPR015424 PyrdxlP-dep_Trfase
IPR015422 PyrdxlP-dep_Trfase_dom1
IPR015421 PyrdxlP-dep_Trfase_major
PfamiView protein in Pfam
PF00155 Aminotran_1_2, 1 hit
SUPFAMiSSF53383 SSF53383, 1 hit
TIGRFAMsiTIGR01141 hisC, 1 hit

Sequencei

Sequence statusi: Complete.

Q5X3Q5-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSIDFQQLPH AGIRSLIPYV PGKSIEELAK EKGITDIIKL ASNENPLGCS
60 70 80 90 100
PLALSAIQTM SSHYIATYPS PWNHPLMSKL ASYLKVKPEQ LFLSNGSDYL
110 120 130 140 150
FNILLNCFAL HTDRHILTHD YAFSTYAIQA NSLQIPINSV PIGHNWEVNI
160 170 180 190 200
TDIVNACNQQ TGIIFIANPN NPTGMLIQQE EIKYLLEQIP KSTLLVLDEA
210 220 230 240 250
YYEFAASQLT VNSLDWLEEH PNLVVTRTFS KIYGMAGLRL GYAIANPSII
260 270 280 290 300
NILKRVQLPF IVNQVALAAA YAAIDDDDFI QSSLKMNNEG MSQLQAGFNE
310 320 330 340 350
LNIKYLHSSC NFLTFDCEED SIALYNYLLD NGIIVRPLHA YKMNNFIRVT
360
IGTKEQNSRF LTALKNFYL
Length:369
Mass (Da):41,489
Last modified:November 23, 2004 - v1
Checksum:i20B46E16A20E4723
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR628336 Genomic DNA Translation: CAH13131.1

Genome annotation databases

EnsemblBacteriaiCAH13131; CAH13131; lpp1979
KEGGilpp:lpp1979

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR628336 Genomic DNA Translation: CAH13131.1

3D structure databases

ProteinModelPortaliQ5X3Q5
SMRiQ5X3Q5
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAH13131; CAH13131; lpp1979
KEGGilpp:lpp1979

Organism-specific databases

LegioListilpp1979

Phylogenomic databases

eggNOGiENOG4105CIH Bacteria
COG0079 LUCA
HOGENOMiHOG000288510
KOiK00817
OMAiPTFDGYP
OrthoDBiPOG091H05S1

Enzyme and pathway databases

UniPathwayi
UPA00031;UER00012

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
IPR004839 Aminotransferase_I/II
IPR005861 HisP_aminotrans
IPR015424 PyrdxlP-dep_Trfase
IPR015422 PyrdxlP-dep_Trfase_dom1
IPR015421 PyrdxlP-dep_Trfase_major
PfamiView protein in Pfam
PF00155 Aminotran_1_2, 1 hit
SUPFAMiSSF53383 SSF53383, 1 hit
TIGRFAMsiTIGR01141 hisC, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiHIS82_LEGPA
AccessioniPrimary (citable) accession number: Q5X3Q5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: November 23, 2004
Last modified: October 10, 2018
This is version 87 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. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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Main funding by: National Institutes of Health

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