Q8U9W3 (HIS8_AGRT5) 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:	Atu3612
ORF Names:	AGR_L_2426

Organism

Agrobacterium tumefaciens (strain C58 / ATCC 33970)

Taxonomic identifier

176299 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Rhizobium/Agrobacterium group › Agrobacterium

Protein attributes

Sequence length	368 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 Reference 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 – 368	368	Histidinol-phosphate aminotransferase HAMAP MF_01023		PRO_0000153292
Amino acid modifications
	Modified residue	224	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8U9W3 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: F7303E731B8193FB	FASTA	368	39,252
	10 20 30 40 50 60 MSAELNQPVP RPGILDIAAY VPGKEHVDGV AKVYKLSSNE TPLGPSPKAI EAFSAAASHL 70 80 90 100 110 120 EIYPDGQAIA LRQAIADVHG LNIANILCGN GSDELLGLLC HVYLGAGDEA IITEHGFLVY 130 140 150 160 170 180 KIQIMGAGAT PVTVKEKDCV VDVDAILAAV TPKTKMVFLA NPGNPTGTYV PVAEIRRLQA 190 200 210 220 230 240 GLPKHVVLVL DAAYAEYVRK NDYEAGLELV SGNRNVVMTR TFSKVYGLAA LRVGWMYAPV 250 260 270 280 290 300 DIIDALNRVR GPFNMSAPAI AAGAAAIRDQ AFVQKAVAHN ALWMEKLVTT FTGLGLTVTP 310 320 330 340 350 360 SVANFILIHF PDQDGKRATD ADEFLSRRGY ILRAVRGYGF PNALRMTVGS EEANLGVIAA LTEFMGQA

References

[1]

"The genome of the natural genetic engineer Agrobacterium tumefaciens C58." Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K., Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y., Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P., Clendenning J. , Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R., Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G., Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y., Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S., Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F., Gordon M.P., Olson M.V., Nester E.W. Science 294:2317-2323(2001) [PubMed: 11743193] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C58 / ATCC 33970.

[2]

"Genome sequence of the plant pathogen and biotechnology agent Agrobacterium tumefaciens C58." Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B., Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K., Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C. , Allinger M., Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C., Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S. Science 294:2323-2328(2001) [PubMed: 11743194] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C58 / ATCC 33970.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE007870 Genomic DNA. Translation: AAK89784.1.
PIR	AB3001. F98282.
RefSeq	NP_356999.1. NC_003063.2.
3D structure databases
ProteinModelPortal	Q8U9W3.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8U9W3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1135486.
GenomeReviews	Gene locus Atu3612 in contig AE007870_GR.
KEGG	atu:Atu3612.
PATRIC	20816696. VBIAgrTum91616_3459.
Phylogenomic databases
eggNOG	COG0079.
HOGENOM	HBG646350.
OMA	GFLVYRI.
ProtClustDB	PRK02731.
Enzyme and pathway databases
BioCyc	ATUM176299-1:ATU3612-MONOMER.
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_AGRT5

Accession

Primary (citable) accession number: Q8U9W3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2002
Last sequence update:	June 1, 2002
Last modified:	January 25, 2012
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program