Q5ZU10 (HIS82_LEGPH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histidinol-phosphate aminotransferase 2
EC=2.6.1.9

Alternative name(s):
Imidazole acetol-phosphate transaminase 2

Gene names

Name:	hisC2
Ordered Locus Names:	lpg1998

Organism

Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513) [Complete proteome] [HAMAP]

Taxonomic identifier

272624 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Legionellaceae › Legionella

Protein attributes

Sequence length	369 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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.
Sequence caution	The sequence AAU28067.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	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 – 369	369	Histidinol-phosphate aminotransferase 2 HAMAP MF_01023		PRO_0000153382
Amino acid modifications
	Modified residue	231	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5ZU10 [UniParc]. Last modified January 10, 2006. Version 2. Checksum: 273B5EFEFE6AC97E	FASTA	369	41,489
	10 20 30 40 50 60 MSIDFQQLPH AGIRSLIPYV PGKSIEELAK EKGITDIIKL ASNENPLGCS PLALSVIQTM 70 80 90 100 110 120 SSHYIATYPS PWNHPLMSKL ASYLKVKPEQ LFLSNGSDYL FNILLNCFAL HTDRHILTHD 130 140 150 160 170 180 YAFSTYAIQA NSLQIPINSV PIGHNWEVNI TDIVNACNQQ TGIIFIANPN NPTGVLIQQE 190 200 210 220 230 240 EIKYLLEQIP KSTLLVLDEA YYEFAASQLT VNSLDWLEEH PNLVVTRTFS KIYGMAGLRL 250 260 270 280 290 300 GYAIANPSII NILKRVQLPF IVNQVALAAA YAAIDDDDFI QSSLKMNNEG MLQLQAGFNE 310 320 330 340 350 360 LNIKYLPSSC NFLTFDCEED SMALYNYLLD NGIIVRPLHA YKMNNFIRVT IGTKEQNSRF LTALKNFYL

References

[1]

"The genomic sequence of the accidental pathogen Legionella pneumophila." Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G., Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V., Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S. , Georghiou A., Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A., Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A., Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A., Russo J.J. Science 305:1966-1968(2004) [PubMed: 15448271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Philadelphia 1 / ATCC 33152 / DSM 7513.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017354 Genomic DNA. Translation: AAU28067.1. Different initiation.
RefSeq	YP_096014.1. NC_002942.5.
3D structure databases
ProteinModelPortal	Q5ZU10.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5ZU10.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3078542.
GenomeReviews	Gene locus lpg1998 in contig AE017354_GR.
KEGG	lpn:lpg1998.
NMPDR	fig|272624.3.peg.834.
PATRIC	22331161. VBILegPne29832_2091.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0079.
HOGENOM	HBG646350.
OMA	ECLDASE.
PhylomeDB	Q5ZU10.
ProtClustDB	PRK02731.
Enzyme and pathway databases
BioCyc	LPNE272624:LPG1998-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

HIS82_LEGPH

Accession

Primary (citable) accession number: Q5ZU10

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2006
Last sequence update:	January 10, 2006
Last modified:	January 25, 2012
This is version 55 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program