Q9PII2 (HIS8_CAMJE) 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:	Cj0317

Organism

Campylobacter jejuni

Taxonomic identifier

197 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length	364 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 – 364

364

Histidinol-phosphate aminotransferase HAMAP MF_01023

PRO_0000153340

Amino acid modifications

Modified residue

226

1

N6-(pyridoxal phosphate)lysine By similarity

Secondary structure

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364

Helix Strand Turn

Details...

Helix

5 – 9

5

Helix

19 – 25

7

Helix

45 – 54

10

Helix

55 – 57

3

Helix

67 – 77

11

Helix

81 – 83

3

Helix

91 – 101

11

Beta strand

107 – 110

4

Helix

117 – 124

8

Beta strand

128 – 131

4

Beta strand

133 – 136

4

Helix

139 – 148

10

Turn

149 – 152

4

Beta strand

153 – 161

9

Helix

171 – 178

8

Beta strand

185 – 190

6

Helix

194 – 200

7

Helix

202 – 204

3

Helix

208 – 214

7

Beta strand

218 – 221

4

Helix

242 – 251

10

Helix

259 – 269

11

Helix

272 – 295

24

Beta strand

304 – 311

8

Beta strand

313 – 315

3

Helix

317 – 325

9

Beta strand

341 – 345

5

Helix

349 – 363

15

Sequences

	Sequence		Length	Mass (Da)
	Q9PII2 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: E1CF525EB38804BC	FASTA	364	41,368
	10 20 30 40 50 60 MKFNEFLNNL SNYEPGKDIE VIAKEYGVKE VIKLASNENP FGTPPKAIEC LRQNANKAHL 70 80 90 100 110 120 YPDDSMIELK STLAQKYKVQ NENIIIGAGS DQVIEFAIHS KLNSKNAFLQ AGVTFAMYEI 130 140 150 160 170 180 YAKQCGAKCY KTQSITHNLD EFKKLYETHK DEIKLIFLCL PNNPLGECLD ASEATEFIKG 190 200 210 220 230 240 VNEDCLVVID AAYNEFASFK DSKKHLEPCE LIKEFDNVLY LGTFSKLYGL GGLRIGYGIA 250 260 270 280 290 300 NANIISAFYK LRAPFNVSNL ALKAAVAAMD DDEFTEKTLE NNFSQMELYK EFAKKHNIKI 310 320 330 340 350 360 IDSYTNFITY FFDEKNSTDL SEKLLKKGII IRNLKSYGLN AIRITIGTSY ENEKFFTEFD KILR

References

[1]

"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences." Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. , van Vliet A.H.M., Whitehead S., Barrell B.G. Nature 403:665-668(2000) [PubMed: 10688204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 11168 / Serotype O:2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AL111168 Genomic DNA. Translation: CAL34468.1.

PIR

A81451.

RefSeq

YP_002343755.1. NC_002163.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3GET	X-ray	2.01	A/B	1-364	[»]

ProteinModelPortal

Q9PII2.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

904641.

GenomeReviews

Gene locus Cj0317 in contig AL111168_GR.

KEGG

cje:Cj0317.

PATRIC

20057551. VBICamJej33762_0309.

Phylogenomic databases

HOGENOM

HBG646350.

OMA

ECLDASE.

ProtClustDB

PRK02731.

Enzyme and pathway databases

BioCyc

CJEJ192222:CJ0317-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_CAMJE

Accession

Primary (citable) accession number: Q9PII2
Secondary accession number(s): Q0PBJ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2002
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program