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Protein

Histidinol-phosphate aminotransferase

Gene

hisC

Organism
Erythrobacter litoralis (strain HTCC2594)
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. Phosphoribosyl-ATP pyrophosphatase (hisE)
  3. Phosphoribosyl-AMP cyclohydrolase (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), Imidazoleglycerol-phosphate synthase, cyclase subunit (ELI_13335), Imidazole glycerol phosphate synthase subunit HisH (hisH)
  6. Imidazoleglycerol-phosphate dehydratase (hisB)
  7. Histidinol-phosphate aminotransferase (hisC)
  8. no protein annotated in this organism
  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:ELI_11415
OrganismiErythrobacter litoralis (strain HTCC2594)
Taxonomic identifieri314225 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesErythrobacteraceaeErythrobacter
Proteomesi
  • UP000008808 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003197571 – 367Histidinol-phosphate aminotransferaseAdd BLAST367

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei221N6-(pyridoxal phosphate)lysineUniRule annotation1

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi314225.ELI_11415.

Structurei

3D structure databases

ProteinModelPortaliQ2N7G6.
SMRiQ2N7G6.
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.
OMAiHGFLVYR.
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.

Q2N7G6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDTRPQIKT WIEGIHAYVP GKATGAQGQA LIKLSANENP LGCSPKALEA
60 70 80 90 100
LDAPGNPATY PDPDAKALRA KLAEVHGLDA GRIVCGTGSD ELLNLAAQAF
110 120 130 140 150
AGPGDEVLFS TYSFSVYDIA ARRCGATPVE APDADYAADV DALLAAVTDK
160 170 180 190 200
TRVVFVANPN NPTGSFLPRD EIARLHAGLP QDVLFVLDQA YAEYLTPEED
210 220 230 240 250
DGGFALAAAH ENVLVTRTFS KAYGLAGERI GWATGAPHFI DALNRVRGPF
260 270 280 290 300
NVTNSGQAAA LAGVDDQNFI DRTRDHNTRE LTRFTDAMAA LGNHGIRPLP
310 320 330 340 350
SKANFALVLF EGTLAAETAL SALADAGYAV RHLPGQGLPH GLRITIGTAE
360
DMDRIARTIA EAAEAAQ
Length:367
Mass (Da):38,651
Last modified:February 7, 2006 - v1
Checksum:iF954B0BF20DEA76B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000157 Genomic DNA. Translation: ABC64375.1.
RefSeqiWP_011415198.1. NC_007722.1.

Genome annotation databases

EnsemblBacteriaiABC64375; ABC64375; ELI_11415.
KEGGieli:ELI_11415.

Similar proteinsi

Entry informationi

Entry nameiHIS8_ERYLH
AccessioniPrimary (citable) accession number: Q2N7G6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: February 7, 2006
Last modified: June 7, 2017
This is version 75 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