Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Histidinol-phosphate aminotransferase

Gene

hisC

Organism
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
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)
  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. Histidinol-phosphatase (hisN)
  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

BioCyciCORYNE:G18NG-11693-MONOMER.
BRENDAi2.6.1.9. 960.
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:Cgl2101, cg2304
OrganismiCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Taxonomic identifieri196627 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesCorynebacteriaceaeCorynebacterium
Proteomesi
  • UP000000582 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001533501 – 366Histidinol-phosphate aminotransferaseAdd BLAST366

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei228N6-(pyridoxal phosphate)lysineUniRule annotation1

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi196627.cg2304.

Structurei

Secondary structure

1366
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 8Combined sources3
Helixi13 – 15Combined sources3
Beta strandi29 – 31Combined sources3
Helixi43 – 56Combined sources14
Helixi57 – 59Combined sources3
Helixi69 – 83Combined sources15
Helixi89 – 91Combined sources3
Beta strandi92 – 96Combined sources5
Helixi97 – 109Combined sources13
Beta strandi115 – 122Combined sources8
Helixi125 – 132Combined sources8
Beta strandi136 – 141Combined sources6
Helixi150 – 160Combined sources11
Beta strandi163 – 170Combined sources8
Turni172 – 174Combined sources3
Helixi180 – 189Combined sources10
Beta strandi191 – 197Combined sources7
Helixi201 – 203Combined sources3
Helixi209 – 212Combined sources4
Turni213 – 215Combined sources3
Turni217 – 219Combined sources3
Beta strandi220 – 228Combined sources9
Helixi233 – 235Combined sources3
Beta strandi238 – 241Combined sources4
Helixi245 – 251Combined sources7
Helixi261 – 272Combined sources12
Helixi274 – 278Combined sources5
Helixi280 – 298Combined sources19
Beta strandi301 – 303Combined sources3
Beta strandi306 – 313Combined sources8
Helixi318 – 327Combined sources10
Beta strandi340 – 344Combined sources5
Helixi348 – 362Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3CQ4X-ray2.20A/B1-366[»]
3CQ5X-ray1.80A/B/C1-366[»]
3CQ6X-ray2.10A/C/E1-366[»]
ProteinModelPortaliQ9KJU4.
SMRiQ9KJU4.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9KJU4.

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.
OMAiPEMNQAL.

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.

Q9KJU4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKITLSDLP LREELRGEHA YGAPQLNVDI RLNTNENPYP PSEALVADLV
60 70 80 90 100
ATVDKIATEL NRYPERDAVE LRDELAAYIT KQTGVAVTRD NLWAANGSNE
110 120 130 140 150
ILQQLLQAFG GPGRTALGFQ PSYSMHPILA KGTHTEFIAV SRGADFRIDM
160 170 180 190 200
DVALEEIRAK QPDIVFVTTP NNPTGDVTSL DDVERIINVA PGIVIVDEAY
210 220 230 240 250
AEFSPSPSAT TLLEKYPTKL VVSRTMSKAF DFAGGRLGYF VANPAFIDAV
260 270 280 290 300
MLVRLPYHLS ALSQAAAIVA LRHSADTLGT VEKLSVERVR VAARLEELGY
310 320 330 340 350
AVVPSESNFV FFGDFSDQHA AWQAFLDRGV LIRDVGIAGH LRTTIGVPEE
360
NDAFLDAAAE IIKLNL
Length:366
Mass (Da):39,918
Last modified:August 13, 2002 - v2
Checksum:i244555DF9A21BDFC
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti68 – 77AVELRDELAA → VWNGDDAWLL in AAF80390 (Ref. 1) Curated10
Sequence conflicti235G → E in AAF80390 (Ref. 1) Curated1
Sequence conflicti254R → P in AAF80390 (Ref. 1) Curated1
Sequence conflicti287 – 288ER → DC in AAF80390 (Ref. 1) Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF160478 Genomic DNA. Translation: AAF80390.1.
AY238320 Genomic DNA. Translation: AAO92311.1.
BA000036 Genomic DNA. Translation: BAB99494.1.
BX927154 Genomic DNA. Translation: CAF20437.1.
RefSeqiNP_601300.1. NC_003450.3.
WP_011014880.1. NC_006958.1.

Genome annotation databases

EnsemblBacteriaiBAB99494; BAB99494; BAB99494.
CAF20437; CAF20437; cg2304.
GeneIDi1020052.
KEGGicgb:cg2304.
cgl:NCgl2020.
PATRICi21496204. VBICorGlu203724_2038.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF160478 Genomic DNA. Translation: AAF80390.1.
AY238320 Genomic DNA. Translation: AAO92311.1.
BA000036 Genomic DNA. Translation: BAB99494.1.
BX927154 Genomic DNA. Translation: CAF20437.1.
RefSeqiNP_601300.1. NC_003450.3.
WP_011014880.1. NC_006958.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3CQ4X-ray2.20A/B1-366[»]
3CQ5X-ray1.80A/B/C1-366[»]
3CQ6X-ray2.10A/C/E1-366[»]
ProteinModelPortaliQ9KJU4.
SMRiQ9KJU4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi196627.cg2304.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB99494; BAB99494; BAB99494.
CAF20437; CAF20437; cg2304.
GeneIDi1020052.
KEGGicgb:cg2304.
cgl:NCgl2020.
PATRICi21496204. VBICorGlu203724_2038.

Phylogenomic databases

eggNOGiENOG4105CIH. Bacteria.
COG0079. LUCA.
HOGENOMiHOG000288510.
KOiK00817.
OMAiPEMNQAL.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00012.
BioCyciCORYNE:G18NG-11693-MONOMER.
BRENDAi2.6.1.9. 960.

Miscellaneous databases

EvolutionaryTraceiQ9KJU4.

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_CORGL
AccessioniPrimary (citable) accession number: Q9KJU4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: August 13, 2002
Last modified: November 30, 2016
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference 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.