P06986 (HIS8_ECOLI) 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
Short name=HPAT
Short name=HspAT

Gene names

Name:	hisC
Ordered Locus Names:	b2021, JW2003

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	356 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.
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.
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 direct assay Ref.2. Source: EcoCyc
Molecular function	L-phenylalanine:2-oxoglutarate aminotransferase activity Inferred from electronic annotation. Source: EC histidinol-phosphate transaminase activity Inferred from direct assay Ref.2. Source: EcoCyc 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 – 356

356

Histidinol-phosphate aminotransferase HAMAP MF_01023

PRO_0000153360

Amino acid modifications

Modified residue

214

1

N6-(pyridoxal phosphate)lysine HAMAP MF_01023

Experimental info

Sequence conflict

130

1

L → P Ref.1

Sequence conflict

130

1

L → P Ref.2

Sequence conflict

149

1

V → A Ref.1

Sequence conflict

149

1

V → A Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

356

Helix Strand Turn

Details...

Helix

6 – 9

4

Helix

12 – 16

5

Turn

27 – 29

3

Beta strand

31 – 33

3

Helix

61 – 71

11

Helix

75 – 77

3

Beta strand

78 – 82

5

Helix

83 – 95

13

Turn

98 – 100

3

Beta strand

102 – 105

4

Beta strand

107 – 109

3

Helix

112 – 120

9

Beta strand

123 – 126

4

Helix

137 – 141

5

Beta strand

147 – 155

9

Turn

157 – 159

3

Helix

165 – 175

11

Turn

176 – 178

3

Beta strand

180 – 184

5

Helix

188 – 190

3

Helix

192 – 194

3

Helix

197 – 199

3

Turn

200 – 202

3

Beta strand

206 – 214

9

Helix

219 – 221

3

Beta strand

224 – 228

5

Helix

230 – 237

8

Helix

247 – 256

10

Helix

259 – 285

27

Beta strand

289 – 292

4

Beta strand

296 – 304

9

Helix

307 – 316

10

Beta strand

333 – 337

5

Helix

341 – 352

12

Sequences

	Sequence		Length	Mass (Da)
	P06986 [UniParc]. Last modified February 1, 1995. Version 2. Checksum: 056CBB3CF894083F	FASTA	356	39,360
	10 20 30 40 50 60 MSTVTITDLA RENVRNLTPY QSARRLGGNG DVWLNANEYP TAVEFQLTQQ TLNRYPECQP 70 80 90 100 110 120 KAVIENYAQY AGVKPEQVLV SRGADEGIEL LIRAFCEPGK DAILYCPPTY GMYSVSAETI 130 140 150 160 170 180 GVECRTVPTL DNWQLDLQGI SDKLDGVKVV YVCSPNNPTG QLINPQDFRT LLELTRGKAI 190 200 210 220 230 240 VVADEAYIEF CPQASLAGWL AEYPHLAILR TLSKAFALAG LRCGFTLANE EVINLLMKVI 250 260 270 280 290 300 APYPLSTPVA DIAAQALSPQ GIVAMRERVA QIIAEREYLI AALKEIPCVE QVFDSETNYI 310 320 330 340 350 LARFKASSAV FKSLWDQGII LRDQNKQPSL SGCLRITVGT REESQRVIDA LRAEQV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure and function of the Salmonella typhimurium and Escherichia coli K-12 histidine operons." Carlomagno M.S., Chiariotti L., Alifano P., Nappo A.G., Bruni C.B. J. Mol. Biol. 203:585-606(1988) [PubMed: 3062174] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Cloning, structure, and expression of the Escherichia coli K-12 hisC gene." Grisolia V., Carlomagno M.S., Nappo A.G., Bruni C.B. J. Bacteriol. 164:1317-1323(1985) [PubMed: 2999081] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[3]	"Nucleotide sequence of the Escherichia coli K12 histidine operon revisited." Jovanovic G., Kostic T., Jankovic M., Savic D.J. J. Mol. Biol. 239:433-435(1994) [PubMed: 8201624] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION. Strain: K12.
[4]	"A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map." Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S. , Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., Horiuchi T. DNA Res. 3:379-392(1996) [PubMed: 9097040] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[6]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]	"Crystal structure of histidinol phosphate aminotransferase (HisC) from Escherichia coli, and its covalent complex with pyridoxal-5'-phosphate and L-histidinol phosphate." Sivaraman J., Li Y., Larocque R., Schrag J.D., Cygler M., Matte A. J. Mol. Biol. 311:761-776(2001) [PubMed: 11518529] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
[8]	"Structures of Escherichia coli histidinol-phosphate aminotransferase and its complexes with histidinol-phosphate and N-(5'-phosphopyridoxyl)-L-glutamate: double substrate recognition of the enzyme." Haruyama K., Nakai T., Miyahara I., Hirotsu K., Mizuguchi H., Hayashi H., Kagamiyama H. Biochemistry 40:4633-4644(2001) [PubMed: 11294630] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 5-351 IN COMPLEX WITH PYRIDOXAL 5'-PHOSPHATE; HISTIDINOL-PHOSPHATE AND N-(5'-PHOSPHOPYRIDOXYL)-L-GLUTAMATE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X03416 Genomic DNA. Translation: CAA27150.1.
X13462 Genomic DNA. Translation: CAA31813.1.
U02071 Unassigned DNA. Translation: AAA19743.1.
U00096 Genomic DNA. Translation: AAC75082.1.
AP009048 Genomic DNA. Translation: BAA15852.1.

PIR

XNECHC. D64967.

RefSeq

NP_416525.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FG3	X-ray	2.20	A	1-356	[»]
1FG7	X-ray	1.50	A	1-356	[»]
1GEW	X-ray	2.00	A	1-356	[»]
1GEX	X-ray	2.20	A	1-356	[»]
1GEY	X-ray	2.30	A	1-356	[»]
1IJI	X-ray	2.20	A	1-356	[»]

ProteinModelPortal

P06986.

SMR

P06986. Positions 3-356.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-9902N.

IntAct

P06986. 5 interactions.

MINT

MINT-1322565.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000000524; EBESCP00000000524; EBESCG00000000442.
EBESCT00000015855; EBESCP00000015146; EBESCG00000014915.

GeneID

946551.

GenomeReviews

Gene locus JW2003 in contig AP009048_GR.
Gene locus b2021 in contig U00096_GR.

KEGG

ecj:JW2003.
eco:b2021.

PATRIC

32119377. VBIEscCol129921_2098.

Organism-specific databases

EchoBASE

EB0441.

EcoGene

EG10446. hisC.

Phylogenomic databases

eggNOG

COG0079.

GeneTree

EBGT00050000008900.

HOGENOM

HBG646350.

OMA

RDQRAVP.

PhylomeDB

P06986.

ProtClustDB

PRK01688.

Enzyme and pathway databases

BioCyc

EcoCyc:HISTPHOSTRANS-MONOMER.
MetaCyc:HISTPHOSTRANS-MONOMER.

Gene expression databases

Genevestigator

P06986.

Family and domain databases

HAMAP

MF_01023. HisC_aminotrans_2.
[Tree]

InterPro

IPR001917. Aminotrans_II_pyridoxalP_BS.
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. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

HIS8_ECOLI

Accession

Primary (citable) accession number: P06986

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	February 1, 1995
Last modified:	January 25, 2012
This is version 126 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program