Q039B8 (Q039B8_LACC3) 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:	LSEI_1426

Organism

Lactobacillus casei (strain ATCC 334) [Complete proteome] [HAMAP] EMBL ABJ70204.1

Taxonomic identifier

321967 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Lactobacillaceae › Lactobacillus

Protein attributes

Sequence length	363 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. HAMAP MF_01023

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis HAMAP MF_01023
Ligand	Pyridoxal phosphate HAMAP MF_01023
Molecular function	Aminotransferase HAMAP MF_01023 EMBL ABJ70204.1 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	224	1	N6-(pyridoxal phosphate)lysine By similarity HAMAP MF_01023

Sequences

	Sequence		Length	Mass (Da)
	Q039B8 [UniParc]. Last modified November 14, 2006. Version 1. Checksum: 0678F9AE70BF5C6B	FASTA	363	40,416
	10 20 30 40 50 60 MLKHTVTHLQ PYIPEKPLAD LAQERALPHI VRMSANENPF GTSDKVQTAI KTWDFTQSRD 70 80 90 100 110 120 YPDGNASRLR SAVAAELGVT ESQLVFGNGL DEIIELIART FLEAGDEVVE PWPTFSEYQL 130 140 150 160 170 180 HAQIEGAKVV NVPVQATTGA FDLEALAQAI TPKTKLLWLC NPNNPTGTLL SLTELEQFLQ 190 200 210 220 230 240 QVPPSVLVLI DEAYIEFTDD YPATSALKLL PNFANLVVLR TFSKIYGLAN FRVGFAVVPE 250 260 270 280 290 300 QLAATMQSVR LPYNLSSVAQ LAAFTALGDQ TFVQTTREQV RQAREDWERF LTKAGLPHYQ 310 320 330 340 350 360 SQTNFQFFQA PQKQAAALKE QLLNHGFLVR DGLKPGWLRI TFGTTAQNIA VQQIMTAFQQ AKK

References

[1]

"Comparative genomics of the lactic acid bacteria." Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V., Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V., Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M., Hawkins T. , Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A., Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W., Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y., Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R., O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T., Richardson P., Kozyavkin S., Weimer B.C., Mills D.A. Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006) [PubMed: 17030793] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000423 Genomic DNA. Translation: ABJ70204.1.
RefSeq	YP_806646.1. NC_008526.1.
3D structure databases
ProteinModelPortal	Q039B8.
ModBase	Search...
Protein-protein interaction databases
STRING	Q039B8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4419749.
GenomeReviews	Gene locus LSEI_1426 in contig CP000423_GR.
KEGG	lca:LSEI_1426.
PATRIC	22206577. VBILacCas62221_1406.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0079.
HOGENOM	HBG646350.
OMA	YEYAEAE.
ProtClustDB	CLSK581767.
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.
ProtoNet	Search...

Entry information

Entry name

Q039B8_LACC3

Accession

Primary (citable) accession number: Q039B8

Entry history

Integrated into UniProtKB/TrEMBL:	November 14, 2006
Last sequence update:	November 14, 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)