Q92A83 (HIS8_LISIN) 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:	lin2039

Organism

Listeria innocua [Complete proteome] [HAMAP]

Taxonomic identifier

1642 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Listeriaceae › Listeria

Protein attributes

Sequence length	360 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
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 – 360

360

Histidinol-phosphate aminotransferase HAMAP MF_01023

PRO_0000153385

Amino acid modifications

Modified residue

222

1

N6-(pyridoxal phosphate)lysine By similarity

Secondary structure

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360

Helix Strand Turn

Details...

Helix

5 – 7

3

Helix

18 – 24

7

Beta strand

35 – 37

3

Helix

45 – 52

8

Helix

67 – 77

11

Helix

81 – 83

3

Helix

91 – 101

11

Beta strand

107 – 114

8

Helix

117 – 124

8

Beta strand

128 – 133

6

Turn

146 – 148

3

Beta strand

153 – 161

9

Helix

171 – 178

8

Beta strand

185 – 190

6

Helix

194 – 196

3

Helix

205 – 209

5

Beta strand

214 – 217

4

Beta strand

220 – 222

3

Helix

238 – 246

9

Helix

259 – 266

8

Turn

268 – 270

3

Helix

274 – 279

6

Helix

283 – 291

9

Beta strand

304 – 308

5

Helix

316 – 322

7

Beta strand

338 – 342

5

Helix

346 – 359

14

Sequences

	Sequence		Length	Mass (Da)
	Q92A83 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 5CB77E883D507F2D	FASTA	360	40,063
	10 20 30 40 50 60 MKWKKSLAGL SSYKPGKREE EVMAELGLTK ITKLSSNENP LGTSKKVAAI QANSSVETEI 70 80 90 100 110 120 YPDGWASSLR KEVADFYQLE EEELIFTAGV DELIELLTRV LLDTTTNTVM ATPTFVQYRQ 130 140 150 160 170 180 NALIEGAEVR EIPLLQDGEH DLEGMLNAID EKTTIVWICN PNNPTGNYIE LADIQAFLDR 190 200 210 220 230 240 VPSDVLVVLD EAYIEYVTPQ PEKHEKLVRT YKNLIITRTF SKIYGLASAR VGYGIADKEI 250 260 270 280 290 300 IRQLNIVRPP FNTTSIGQKL AIEAIKDQAF IGECRTSNAN GIKQYEAFAK RFEKVKLYPA 310 320 330 340 350 360 NGNFVLIDLG IEAGTIFSYL EKNGYITRSG AALGFPTAVR ITIGKEEDNS AVIALLEKLL

References

[1]

"Comparative genomics of Listeria species." Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E., Dominguez-Bernal G., Duchaud E. , Durant L., Dussurget O., Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P. Science 294:849-852(2001) [PubMed: 11679669] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CLIP 11262 / Serovar 6a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AL596170 Genomic DNA. Translation: CAC97269.1.

PIR

AE1687.

RefSeq

NP_471373.1. NC_003212.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3FFH	X-ray	2.31	A/B	1-360	[»]

ProteinModelPortal

Q92A83.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

1130749.

GenomeReviews

Gene locus lin2039 in contig AL592022_GR.

KEGG

lin:lin2039.

NMPDR

fig|272626.1.peg.2026.

PATRIC

20300889. VBILisInn102668_2083.

Organism-specific databases

GenoList

LIN2039.

CMR

Search...

Phylogenomic databases

HOGENOM

HBG646350.

OMA

YIELADI.

ProtClustDB

PRK03158.

Enzyme and pathway databases

BioCyc

LINN272626:LIN2039-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_LISIN

Accession

Primary (citable) accession number: Q92A83

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2002
Last sequence update:	December 1, 2001
Last modified:	January 25, 2012
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program