Q145X5 (Q145X5_BURXL) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Histidinol-phosphate aminotransferase 1 HAMAP MF_01023
EC=2.6.1.9 HAMAP MF_01023

Alternative name(s):
Imidazole acetol-phosphate transaminase 1 HAMAP MF_01023

Gene names

Name:	hisC1 HAMAP MF_01023
Ordered Locus Names:	Bxeno_A0326
ORF Names:	Bxe_A4136 EMBL ABE28864.1

Organism

Burkholderia xenovorans (strain LB400) [Complete proteome] [HAMAP]

Taxonomic identifier

266265 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia

Protein attributes

Sequence length	359 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 SAAS SAAS005861
Cofactor	Pyridoxal phosphate By similarity. HAMAP MF_01023 SAAS SAAS005861
Pathway	Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. HAMAP MF_01023 SAAS SAAS005861
Subunit structure	Homodimer By similarity. HAMAP MF_01023
Sequence similarities	Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily. HAMAP MF_01023

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis HAMAP MF_01023 SAAS SAAS005861
Ligand	Pyridoxal phosphate HAMAP MF_01023 SAAS SAAS005861
Molecular function	Aminotransferase HAMAP MF_01023 SAAS SAAS005861 EMBL ABE28864.1 Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	histidine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	L-phenylalanine:2-oxoglutarate aminotransferase activity Inferred from electronic annotation. Source: EC histidinol-phosphate transaminase activity Inferred from electronic annotation. Source: HAMAP 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
Amino acid modifications
	Modified residue	213	1	N6-(pyridoxal phosphate)lysine By similarity HAMAP MF_01023

Sequences

	Sequence		Length	Mass (Da)
	Q145X5 [UniParc]. Last modified August 22, 2006. Version 1. Checksum: 4C41DC13BDF44D3E	FASTA	359	39,737
	10 20 30 40 50 60 MSRYWSDIVH RLTPYVPGEQ PVVTHPVKLN TNENPYPPSP RVLEAIRQEL GDAAESLRRY 70 80 90 100 110 120 PDPTAQKLRE TVAAYHGIRA EQVFAGNGSD EVLALTFQAL LKHDKPLLFP DVTYSFYPTY 130 140 150 160 170 180 ARLFEVDYRT IPLDDSFTIH VDDYMSPNGG ILFPNPNAPT GRPLPLADIE RLVASSPDSV 190 200 210 220 230 240 VVIDEAYVDF GAQSAIGLID RYPNLLVVQT VSKSRSLAGM RVGFAFGNPD LIGALNRVKD 250 260 270 280 290 300 SFNSYPLDRL AQAAAAAAYE DDAWFRDTCA KVVASRERLA AGLTALGFEV LPSAANLLFA 310 320 330 340 350 RHEGYDAATL ALRLRDKEIF VRHFKAPRID QHLRISVGTD AECDILLDAL RDIFSAYVG

References

[1]

"Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome shaped for versatility." Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L., Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J., Parnell J.J. , Ramette A., Richardson P., Seeger M., Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M. Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006) [PubMed: 17030797] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000270 Genomic DNA. Translation: ABE28864.1.
RefSeq	YP_556916.1. NC_007951.1.
3D structure databases
ProteinModelPortal	Q145X5.
ModBase	Search...
Protein-protein interaction databases
STRING	Q145X5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4003425.
GenomeReviews	Gene locus Bxeno_A0326 in contig CP000270_GR.
KEGG	bxe:Bxe_A4136.
PATRIC	19326009. VBIBurXen52548_0346.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG646350.
OMA	IGRREEM.
PhylomeDB	Q145X5.
ProtClustDB	PRK05387.
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

Q145X5_BURXL

Accession

Primary (citable) accession number: Q145X5

Entry history

Integrated into UniProtKB/TrEMBL:	August 22, 2006
Last sequence update:	August 22, 2006
Last modified:	December 14, 2011
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)