Q51687 (HIS8_PARDP) 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
Synonyms:	hisH
Ordered Locus Names:	Pden_1409

Organism

Paracoccus denitrificans (strain Pd 1222) [Complete proteome] [HAMAP]

Taxonomic identifier

318586 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Paracoccus

Protein attributes

Sequence length	367 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 – 367	367	Histidinol-phosphate aminotransferase HAMAP MF_01023		PRO_0000153409
Amino acid modifications
	Modified residue	221	1	N6-(pyridoxal phosphate)lysine By similarity
Experimental info
	Sequence conflict	9	1	A → R in CAA96498. Ref.1
	Sequence conflict	153	1	Missing in CAA96498. Ref.1
	Sequence conflict	163	1	N → K in CAA96498. Ref.1
	Sequence conflict	185 – 186	2	AI → RIA in CAA96498. Ref.1
	Sequence conflict	205	1	E → Q in CAA96498. Ref.1
	Sequence conflict	208 – 209	2	TR → QA in CAA96498. Ref.1
	Sequence conflict	248	1	G → A in CAA96498. Ref.1
	Sequence conflict	357 – 363	7	GQYMAER → ASTWPSA in CAA96498. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q51687 [UniParc]. Last modified March 6, 2007. Version 2. Checksum: 49C86EA0501EB76B	FASTA	367	39,582
	10 20 30 40 50 60 MSQNQTTIAP QPGIMEISLY EGGASKVAGV ENVVKLSSNE NPFGPSDKAR EAMIRAAHGL 70 80 90 100 110 120 HRYPNTDHAG LRGAIGEVHG LDPDRIICGV GSDEIIHFLC QAYAGPGTEV LFTEHGFLMY 130 140 150 160 170 180 RISAHAAGAI PVQVAERDRV TDIDALIAGA TPRTRLIFVA NPNNPTGTMV GLPELERLAR 190 200 210 220 230 240 AVPQAILVVD AAYAEYVGDY DGGAELATRL PNVFMTRTFS KIYGLGGLRV GWGYGPREIV 250 260 270 280 290 300 DVLNRIRGPF NLSNVALEGA EAAMRDREHI ARCQAENARM RAWLAEALAE KGVPSDTSCA 310 320 330 340 350 360 NFILARFADA ETAGACDEYL KTQGLIVRRV AGYGLPHCLR ITIGDEASCR RVAHVIGQYM AERAESR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Paracoccus denitrificans ccmA, B and C genes: cloning and sequencing, and analysis of the potential of their products to form a haem or apo-c-type cytochrome transporter." Page D., Pearce D.A., Norris H.A., Ferguson S.J. Microbiology 143:563-576(1997) [PubMed: 9043133] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. , Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M., Richardson P. Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Pd 1222.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z71971 Genomic DNA. Translation: CAA96498.1. CP000489 Genomic DNA. Translation: ABL69510.1.
RefSeq	YP_915206.1. NC_008686.1.
3D structure databases
ProteinModelPortal	Q51687.
ModBase	Search...
Protein-protein interaction databases
STRING	Q51687.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4581274.
GenomeReviews	Gene locus Pden_1409 in contig CP000489_GR.
KEGG	pde:Pden_1409.
PATRIC	22853967. VBIParDen97112_1374.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0079.
HOGENOM	HBG646350.
OMA	GFLVYRI.
PhylomeDB	Q51687.
ProtClustDB	PRK02731.
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_PARDP

Accession

Primary (citable) accession number: Q51687
Secondary accession number(s): A1B1W6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2002
Last sequence update:	March 6, 2007
Last modified:	January 25, 2012
This is version 69 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program