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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

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 366366Histidinol-phosphate aminotransferasePRO_0000153350Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei228 – 2281N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi196627.cg2304.

Structurei

Secondary structure

1
366
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 83Combined sources
Helixi13 – 153Combined sources
Beta strandi29 – 313Combined sources
Helixi43 – 5614Combined sources
Helixi57 – 593Combined sources
Helixi69 – 8315Combined sources
Helixi89 – 913Combined sources
Beta strandi92 – 965Combined sources
Helixi97 – 10913Combined sources
Beta strandi115 – 1228Combined sources
Helixi125 – 1328Combined sources
Beta strandi136 – 1416Combined sources
Helixi150 – 16011Combined sources
Beta strandi163 – 1708Combined sources
Turni172 – 1743Combined sources
Helixi180 – 18910Combined sources
Beta strandi191 – 1977Combined sources
Helixi201 – 2033Combined sources
Helixi209 – 2124Combined sources
Turni213 – 2153Combined sources
Turni217 – 2193Combined sources
Beta strandi220 – 2289Combined sources
Helixi233 – 2353Combined sources
Beta strandi238 – 2414Combined sources
Helixi245 – 2517Combined sources
Helixi261 – 27212Combined sources
Helixi274 – 2785Combined sources
Helixi280 – 29819Combined sources
Beta strandi301 – 3033Combined sources
Beta strandi306 – 3138Combined sources
Helixi318 – 32710Combined sources
Beta strandi340 – 3445Combined sources
Helixi348 – 36215Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CQ4X-ray2.20A/B1-366[»]
3CQ5X-ray1.80A/B/C1-366[»]
3CQ6X-ray2.10A/C/E1-366[»]
ProteinModelPortaliQ9KJU4.
SMRiQ9KJU4. Positions 1-366.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti68 – 7710AVELRDELAA → VWNGDDAWLL in AAF80390 (Ref. 1) Curated
Sequence conflicti235 – 2351G → E in AAF80390 (Ref. 1) Curated
Sequence conflicti254 – 2541R → P in AAF80390 (Ref. 1) Curated
Sequence conflicti287 – 2882ER → DC in AAF80390 (Ref. 1) Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
3CQ4X-ray2.20A/B1-366[»]
3CQ5X-ray1.80A/B/C1-366[»]
3CQ6X-ray2.10A/C/E1-366[»]
ProteinModelPortaliQ9KJU4.
SMRiQ9KJU4. Positions 1-366.
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.
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: September 7, 2016
This is version 111 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.