Q9KJU4 (HIS8_CORGL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histidinol-phosphate aminotransferase
EC=2.6.1.9

Alternative name(s):
Imidazole acetol-phosphate transaminase

Gene names

Name:	hisC
Ordered Locus Names:	Cgl2101, cg2304

Organism

Corynebacterium glutamicum (Brevibacterium flavum)

Taxonomic identifier

1718 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

Protein attributes

Sequence length	366 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	L-histidinol phosphate + 2-oxoglutarate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate. HAMAP MF_01023
Cofactor	Pyridoxal phosphate By similarity. HAMAP MF_01023
Pathway	Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. HAMAP MF_01023
Subunit structure	Homodimer By similarity. HAMAP MF_01023
Sequence similarities	Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	histidine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	L-phenylalanine:2-oxoglutarate aminotransferase activity Inferred from electronic annotation. Source: EC histidinol-phosphate transaminase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 366

366

Histidinol-phosphate aminotransferase HAMAP MF_01023

PRO_0000153350

Amino acid modifications

Modified residue

228

1

N6-(pyridoxal phosphate)lysine By similarity

Experimental info

Sequence conflict

68 – 77

10

AVELRDELAA → VWNGDDAWLL in AAF80390. Ref.1

Sequence conflict

235

1

G → E in AAF80390. Ref.1

Sequence conflict

254

1

R → P in AAF80390. Ref.1

Sequence conflict

287 – 288

2

ER → DC in AAF80390. Ref.1

Secondary structure

1

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366

Helix Strand Turn

Details...

Helix

6 – 8

3

Helix

13 – 15

3

Helix

43 – 57

15

Helix

69 – 83

15

Helix

89 – 91

3

Beta strand

92 – 97

6

Helix

98 – 109

12

Beta strand

115 – 121

7

Beta strand

123 – 125

3

Helix

127 – 133

7

Beta strand

136 – 141

6

Helix

150 – 160

11

Beta strand

163 – 170

8

Turn

172 – 174

3

Helix

180 – 189

10

Beta strand

191 – 197

7

Helix

201 – 203

3

Helix

209 – 212

4

Turn

213 – 215

3

Turn

217 – 219

3

Beta strand

220 – 226

7

Turn

227 – 229

3

Beta strand

238 – 241

4

Helix

244 – 250

7

Turn

251 – 253

3

Helix

261 – 272

12

Helix

274 – 298

25

Beta strand

307 – 313

7

Helix

318 – 327

10

Beta strand

340 – 344

5

Helix

348 – 361

14

Sequences

	Sequence		Length	Mass (Da)
	Q9KJU4 [UniParc]. Last modified August 13, 2002. Version 2. Checksum: 244555DF9A21BDFC	FASTA	366	39,918
	10 20 30 40 50 60 MTKITLSDLP LREELRGEHA YGAPQLNVDI RLNTNENPYP PSEALVADLV ATVDKIATEL 70 80 90 100 110 120 NRYPERDAVE LRDELAAYIT KQTGVAVTRD NLWAANGSNE ILQQLLQAFG GPGRTALGFQ 130 140 150 160 170 180 PSYSMHPILA KGTHTEFIAV SRGADFRIDM DVALEEIRAK QPDIVFVTTP NNPTGDVTSL 190 200 210 220 230 240 DDVERIINVA PGIVIVDEAY AEFSPSPSAT TLLEKYPTKL VVSRTMSKAF DFAGGRLGYF 250 260 270 280 290 300 VANPAFIDAV MLVRLPYHLS ALSQAAAIVA LRHSADTLGT VEKLSVERVR VAARLEELGY 310 320 330 340 350 360 AVVPSESNFV FFGDFSDQHA AWQAFLDRGV LIRDVGIAGH LRTTIGVPEE NDAFLDAAAE IIKLNL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of hisC gene from Corynebacterium glutamicum." Han M.S., Jung S.I., Chun J.Y., Lee M.-S. Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613.
[2]	"Genome-based analysis of biosynthetic aminotransferase genes of Corynebacterium glutamicum." McHardy A.C., Tauch A., Rueckert C., Puehler A., Kalinowski J. J. Biotechnol. 104:229-240(2003) [PubMed: 12948641] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[3]	"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032." Nakagawa S. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[4]	"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins." Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A. J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF160478 Genomic DNA. Translation: AAF80390.1.
AY238320 Genomic DNA. Translation: AAO92311.1.
BA000036 Genomic DNA. Translation: BAB99494.1.
BX927154 Genomic DNA. Translation: CAF20437.1.

RefSeq

NP_601300.1. NC_003450.3.
YP_226338.1. NC_006958.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3CQ4	X-ray	2.20	A/B	1-366	[»]
3CQ5	X-ray	1.80	A/B/C	1-366	[»]
3CQ6	X-ray	2.10	A/C/E	1-366	[»]

ProteinModelPortal

Q9KJU4.

SMR

Q9KJU4. Positions 1-366.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

1020052.
3345122.

GenomeReviews

Gene locus Cgl2101 in contig BA000036_GR.
Gene locus cg2304 in contig BX927147_GR.

KEGG

cgb:cg2304.
cgl:NCgl2020.

PATRIC

21496204. VBICorGlu203724_2038.

Phylogenomic databases

HOGENOM

HBG646350.

OMA

GRTAIGF.

PhylomeDB

Q9KJU4.

ProtClustDB

PRK03317.

Enzyme and pathway databases

BioCyc

CGLU196627:CG2304-MONOMER.

Family and domain databases

HAMAP

MF_01023. HisC_aminotrans_2.
[Tree]

InterPro

IPR004839. Aminotransferase_I/II.
IPR005861. HisP_aminotrans.
IPR015424. PyrdxlP-dep_Trfase_major_dom.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]

Gene3D

G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit.

KO

K00817.

Pfam

PF00155. Aminotran_1_2. 1 hit.
[Graphical view]

SUPFAM

SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.

TIGRFAMs

TIGR01141. HisC. 1 hit.

PROSITE

PS00599. AA_TRANSFER_CLASS_2. False negative.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

HIS8_CORGL

Accession

Primary (citable) accession number: Q9KJU4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2002
Last sequence update:	August 13, 2002
Last modified:	January 25, 2012
This is version 79 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program