A9H311 (HIS8_GLUDA) 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:	GDI0282, Gdia_2345

Organism

Gluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / PAl5) [Complete proteome] [HAMAP]

Taxonomic identifier

272568 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Acetobacteraceae › Gluconacetobacter

Protein attributes

Sequence length	356 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 – 356	356	Histidinol-phosphate aminotransferase HAMAP MF_01023		PRO_1000084195
Amino acid modifications
	Modified residue	210	1	N6-(pyridoxal phosphate)lysine By similarity
Experimental info
	Sequence conflict	315	1	A → G in ACI52099. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	A9H311 [UniParc]. Last modified February 5, 2008. Version 1. Checksum: 8B182EEC073DD851	FASTA	356	39,008
	10 20 30 40 50 60 MSRFWSPVVH RLTPYVPGEQ PKLTNLIKLN TNESPYGPPP GALEAIRAAA DDTLRLYSDP 70 80 90 100 110 120 TSERLRAAIA QAHDVGMDEI FVGNGSDEVL AHAFHALLQH DAPLLTPDIT YSFYPVYCGL 130 140 150 160 170 180 YGIAHQPVPL DDAMRIDVDD YRRPCAGLVL PNPNAPTGIA LGLGQIETLL RAQPDRVVVI 190 200 210 220 230 240 DEAYVDFGAD TAIPLVRRFP NLLVVRTLSK SHALAGLRVG YAIGHPDLVE ALNRVKDSFN 250 260 270 280 290 300 SYPLDRLAQA GAAAAIADRE WLARTTGKII KTRIGLTSSL RGLGFEVLPS QANFVFARHP 310 320 330 340 350 DRDAAHLAAA LRERAIIVRH FRTPRIAEWL RITVGTDEEC RVLTDALGTI LTRNAD

References

[1]

"Gluconacetobacter diazotrophicus Pal5 complete genome." Bertalan M., Baldani I.J., Ferreira P. Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49037 / DSM 5601 / PAl5.

[2]

"Complete sequence of chromosome of Gluconacetobacter diazotrophicus PAl 5." US DOE Joint Genome Institute Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Triplett E.W. Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49037 / DSM 5601 / PAl5.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM889285 Genomic DNA. Translation: CAP54225.1. CP001189 Genomic DNA. Translation: ACI52099.1.
RefSeq	YP_001600571.1. NC_010125.1. YP_002276714.1. NC_011365.1.
3D structure databases
ProteinModelPortal	A9H311.
ModBase	Search...
Protein-protein interaction databases
STRING	A9H311.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5788912. 6975775.
GenomeReviews	Gene locus GDI0282 in contig AM889285_GR. Gene locus Gdia_2345 in contig CP001189_GR.
KEGG	gdi:GDI_0282. gdj:Gdia_2345.
PATRIC	22053152. VBIGluDia203729_2355.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG646350.
OMA	SSANFVF.
ProtClustDB	PRK05387.
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_GLUDA

Accession

Primary (citable) accession number: A9H311
Secondary accession number(s): B5ZF55

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	February 5, 2008
Last modified:	January 25, 2012
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program