Q1LT68 (HIS8_BAUCH) 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:	BCI_0403

Organism

Baumannia cicadellinicola subsp. Homalodisca coagulata [Complete proteome] [HAMAP]

Taxonomic identifier

374463 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Candidatus Baumannia

Protein attributes

Sequence length	360 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 – 360	360	Histidinol-phosphate aminotransferase HAMAP MF_01023		PRO_1000063463
Amino acid modifications
	Modified residue	213	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1LT68 [UniParc]. Last modified May 30, 2006. Version 1. Checksum: 7CF6EB03501FD99E	FASTA	360	40,496
	10 20 30 40 50 60 MSILNLARTN VLTLEPYQSA RRIGGGSQGN IWLNANEYPQ PTFYMLRSSN LNRYPDCQPQ 70 80 90 100 110 120 ELLNSYAAYA GVQPNQVLAC RGADEGIELL IRTFCEPSKD KILFCPPTYG MYRVSAETFG 130 140 150 160 170 180 VAYCAIQALD NWQLDLDTIY AQLDCVKLIY ICHPNNPTGN IINPSDIRQL LDITHGRTIL 190 200 210 220 230 240 VVDEAYIDFY PTASISSWIN HYPHLVILRT LSKAFALAGL RCGFILANPD IIKLLLKVIA 250 260 270 280 290 300 PYPISRPVVD IAKQALSTKG IHQTKRRVAN IDINRNWLIQ QLAECSCVSV VFPSVTNYLL 310 320 330 340 350 360 VRFHPNYHVF QSLWKKGTIL RDQNQQIGLA NCLRITIGTS LECQNLLTAL QALTLVSHKE

References

[1]

"Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters." Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A. PLoS Biol. 4:1079-1092(2006) [PubMed: 16729848] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000238 Genomic DNA. Translation: ABF14107.1.
RefSeq	YP_588846.1. NC_007984.1.
3D structure databases
ProteinModelPortal	Q1LT68.
SMR	Q1LT68. Positions 1-352.
ModBase	Search...
Protein-protein interaction databases
STRING	Q1LT68.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4056522.
GenomeReviews	Gene locus BCI_0403 in contig CP000238_GR.
KEGG	bci:BCI_0403.
PATRIC	21074313. VBIBauCic75062_0385.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0079.
HOGENOM	HBG646350.
OMA	PMEDIER.
PhylomeDB	Q1LT68.
Enzyme and pathway databases
BioCyc	BCIC186490:BCI_0403-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_BAUCH

Accession

Primary (citable) accession number: Q1LT68

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	May 30, 2006
Last modified:	January 25, 2012
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program