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Protein

Histidinol-phosphate aminotransferase

Gene

hisC

Organism
Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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), ATP phosphoribosyltransferase regulatory subunit (hisZ)
  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 HisF (hisF), 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

Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesis

Keywords - Ligandi

Pyridoxal 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:lin2039
OrganismiListeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262)
Taxonomic identifieri272626 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria
Proteomesi
  • UP000002513 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001533851 – 360Histidinol-phosphate aminotransferaseAdd BLAST360

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei222N6-(pyridoxal phosphate)lysineUniRule annotation1

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi272626.lin2039.

Structurei

Secondary structure

1360
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 7Combined sources3
Helixi18 – 24Combined sources7
Turni25 – 27Combined sources3
Helixi45 – 52Combined sources8
Helixi67 – 77Combined sources11
Helixi81 – 83Combined sources3
Beta strandi84 – 89Combined sources6
Helixi90 – 101Combined sources12
Beta strandi107 – 114Combined sources8
Helixi117 – 125Combined sources9
Beta strandi128 – 133Combined sources6
Helixi142 – 148Combined sources7
Beta strandi153 – 161Combined sources9
Turni163 – 165Combined sources3
Helixi171 – 178Combined sources8
Beta strandi185 – 190Combined sources6
Helixi194 – 196Combined sources3
Helixi205 – 209Combined sources5
Beta strandi214 – 222Combined sources9
Beta strandi232 – 236Combined sources5
Helixi238 – 246Combined sources9
Helixi255 – 266Combined sources12
Helixi268 – 291Combined sources24
Beta strandi302 – 308Combined sources7
Helixi313 – 322Combined sources10
Turni330 – 334Combined sources5
Beta strandi338 – 342Combined sources5
Helixi346 – 359Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3FFHX-ray2.31A/B1-360[»]
ProteinModelPortaliQ92A83.
SMRiQ92A83.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ92A83.

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.
OMAiVWPPESY.
OrthoDBiPOG091H05S1.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_01023. HisC_aminotrans_2. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR005861. HisP_aminotrans.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01141. hisC. 1 hit.

Sequencei

Sequence statusi: Complete.

Q92A83-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKWKKSLAGL SSYKPGKREE EVMAELGLTK ITKLSSNENP LGTSKKVAAI
60 70 80 90 100
QANSSVETEI YPDGWASSLR KEVADFYQLE EEELIFTAGV DELIELLTRV
110 120 130 140 150
LLDTTTNTVM ATPTFVQYRQ NALIEGAEVR EIPLLQDGEH DLEGMLNAID
160 170 180 190 200
EKTTIVWICN PNNPTGNYIE LADIQAFLDR VPSDVLVVLD EAYIEYVTPQ
210 220 230 240 250
PEKHEKLVRT YKNLIITRTF SKIYGLASAR VGYGIADKEI IRQLNIVRPP
260 270 280 290 300
FNTTSIGQKL AIEAIKDQAF IGECRTSNAN GIKQYEAFAK RFEKVKLYPA
310 320 330 340 350
NGNFVLIDLG IEAGTIFSYL EKNGYITRSG AALGFPTAVR ITIGKEEDNS
360
AVIALLEKLL
Length:360
Mass (Da):40,063
Last modified:December 1, 2001 - v1
Checksum:i5CB77E883D507F2D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL596170 Genomic DNA. Translation: CAC97269.1.
PIRiAE1687.
RefSeqiWP_010991721.1. NC_003212.1.

Genome annotation databases

EnsemblBacteriaiCAC97269; CAC97269; CAC97269.
KEGGilin:hisC.
PATRICi20300889. VBILisInn102668_2083.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL596170 Genomic DNA. Translation: CAC97269.1.
PIRiAE1687.
RefSeqiWP_010991721.1. NC_003212.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3FFHX-ray2.31A/B1-360[»]
ProteinModelPortaliQ92A83.
SMRiQ92A83.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272626.lin2039.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAC97269; CAC97269; CAC97269.
KEGGilin:hisC.
PATRICi20300889. VBILisInn102668_2083.

Phylogenomic databases

eggNOGiENOG4105CIH. Bacteria.
COG0079. LUCA.
HOGENOMiHOG000288510.
KOiK00817.
OMAiVWPPESY.
OrthoDBiPOG091H05S1.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00012.

Miscellaneous databases

EvolutionaryTraceiQ92A83.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_01023. HisC_aminotrans_2. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR005861. HisP_aminotrans.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01141. hisC. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiHIS8_LISIN
AccessioniPrimary (citable) accession number: Q92A83
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: December 1, 2001
Last modified: November 2, 2016
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.