Reviewed, UniProtKB/Swiss-Prot Q57004 (HIS82_HAEIN)

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:	HI1166

Organism

Haemophilus influenzae [Complete proteome] [HAMAP]

Taxonomic identifier

727 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length	366 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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.
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	Complete proteome
Gene Ontology (GO)
Biological process	histidine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	1-aminocyclopropane-1-carboxylate synthase activity Inferred from electronic annotation. Source: InterPro histidinol-phosphate transaminase activity Inferred from electronic annotation. Source: HAMAP 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 2 HAMAP MF_01023		PRO_0000153369
Amino acid modifications
	Modified residue	226	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q57004-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 8E671105AD669B05	FASTA	366	41,053
	10 20 30 40 50 60 MQYINIANRG VKSLSPYQAG KPIEELEREL GISNIVKLAS NENPFGFPES AKKAIFEQLD 70 80 90 100 110 120 KLTRYPDANG FELKQTIAKK FGVQPNQITL GNGSNDLLEL FAHTFATEGD EIMYSQYAFI 130 140 150 160 170 180 VYPLVTKAIN AIVKEIPAKN WGHDLQGFLT ALSDKTKLIY IANPNNPTGN FLTSQEIEDF 190 200 210 220 230 240 LAEVPENVIV VLDEAYTEFT RSEERVDSFS LLKKYSNLII SRSLSKAYGL AGLRIGYAVS 250 260 270 280 290 300 NPEIADLLNR VRQPFNCNSL ALTAAVAVMN DDKFVEKVAE NNRIEMRRYE DFCQKNQLDY 310 320 330 340 350 360 IPSKGNFITI DFKQPAAPIY DALLREGVIV RPIAGYGMPN HLRISIGLPE ENDKFFTALS KVLKFA

References

[1]

"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed: 7542800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L42023 Genomic DNA. Translation: AAC22821.1.
PIR	D64187.
RefSeq	NP_439324.1.
3D structure databases
HSSP	HSSP built from PDB template 1FG7 based on UniProtKB P06986.
ModBase	Search...
Genome annotation databases
GeneID	950769.
GenomeReviews	Gene locus HI1166 in contig L42023_GR.
KEGG	hin:HI1166.
NMPDR	fig|71421.1.peg.1119.
TIGR	HI1166.
Phylogenomic databases
HOGENOM	Q57004.
OMA	KGYIVRS.
Enzyme and pathway databases
BioCyc	HINF71421:HI_1166-MON.
BRENDA	2.6.1.9. 109.
Family and domain databases
HAMAP	MF_01023. [Tree]
InterPro	IPR001176. ACC_synthase. IPR004839. Aminotransferase_I/II. IPR005861. HisP_aminotrans. IPR004838. NHTrfase_class1_PyrdxlP-BS. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
Pfam	PF00155. Aminotran_1_2. 1 hit. [Graphical view]
PRINTS	PR00753. ACCSYNTHASE.
TIGRFAMs	TIGR01141. hisC. 1 hit.
PROSITE	PS00105. AA_TRANSFER_CLASS_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HIS82_HAEIN

Accession

Primary (citable) accession number: Q57004
Secondary accession number(s): P96340

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	November 3, 2009
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)