Q9ZHE5 (HIS8_BUCAP) 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:	BUsg_094

Organism

Buchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]

Taxonomic identifier

198804 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	355 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.

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 – 355	355	Histidinol-phosphate aminotransferase HAMAP MF_01023		PRO_0000153333
Amino acid modifications
	Modified residue	214	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9ZHE5 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: C919301FE84D6DC8	FASTA	355	40,474
	10 20 30 40 50 60 MTANINKLAR KNIQKLNPYQ SARRIGGKGD TWLNANESPI SVPFKGKVKV FNRYPECQPN 70 80 90 100 110 120 NLLSSYANYV GLLNNQILVT RGADEGIELL IKAFCEPGKD AIIYCPPTYD MYAINAKIAN 130 140 150 160 170 180 VEIKEIPTFK NTWKIDLLNI RSNLNKVKLI YICNPNNPTG NIVSQEDLKS LLKVTLGQSL 190 200 210 220 230 240 VIIDEAYIEF SPKNSMVNYL KTFPNLIILR TLSKAFALAG IRCGFTLAQK EVIDILHKVI 250 260 270 280 290 300 SPYPISTLIA DIAVQSLEKK AIDDMKNRVL KLNMNRIWLI DELKKISCVK KVFDSHANYI 310 320 330 340 350 LVEFYMFKKI FQSLWQKGII LRNQNHKNNL KNCLRISIGS KSECMRLVQE LKNFI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Buchnera aphidicola (Aphid endosymbiont) contains genes encoding enzymes of histidine biosynthesis." Clark M.A., Baumann L., Baumann P. Curr. Microbiol. 37:356-358(1998) [PubMed: 9767718] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"50 million years of genomic stasis in endosymbiotic bacteria." Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E. Science 296:2376-2379(2002) [PubMed: 12089438] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sg.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF067228 Genomic DNA. Translation: AAC97356.1. AE013218 Genomic DNA. Translation: AAM67664.1.
RefSeq	NP_660453.1. NC_004061.1.
3D structure databases
ProteinModelPortal	Q9ZHE5.
SMR	Q9ZHE5. Positions 2-353.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBUCT00000000472; EBBUCP00000000472; EBBUCG00000000472.
GeneID	1005911.
GenomeReviews	Gene locus BUsg_094 in contig AE013218_GR.
KEGG	bas:BUsg094.
PATRIC	21246965. VBIBucAph100086_0097.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000007997.
HOGENOM	HBG646350.
OMA	RDQRAVP.
ProtClustDB	PRK01688.
Enzyme and pathway databases
BioCyc	BAPH198804:BUSG094-MONOMER.
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_BUCAP

Accession

Primary (citable) accession number: Q9ZHE5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 1, 1999
Last modified:	January 25, 2012
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program