C7NAE4 (C7NAE4_LEPBD) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

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

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

Gene names

Name:	hisC HAMAP-Rule MF_01023
Ordered Locus Names:	Lebu_1235

Organism

Leptotrichia buccalis (strain ATCC 14201 / DSM 1135 / JCM 12969 / NCTC 10249) [Complete proteome] [HAMAP]

Taxonomic identifier

523794 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Fusobacteria › Fusobacteriia › Fusobacteriales › Leptotrichiaceae › Leptotrichia › Leptotrichia buccalis

Protein attributes

Sequence length	357 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-Rule MF_01023 SAAS SAAS005861
Cofactor	Pyridoxal phosphate By similarity. HAMAP-Rule 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-Rule MF_01023 SAAS SAAS005861
Subunit structure	Homodimer By similarity. HAMAP-Rule MF_01023
Sequence similarities	Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily. HAMAP-Rule MF_01023

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis HAMAP-Rule MF_01023 SAAS SAAS005861
Ligand	Pyridoxal phosphate HAMAP-Rule MF_01023 SAAS SAAS005861
Molecular function	Aminotransferase HAMAP-Rule MF_01023 SAAS SAAS005861 EMBL ACV39125.1 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	216	1	N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01023

Sequences

	Sequence		Length	Mass (Da)
	C7NAE4 [UniParc]. Last modified October 13, 2009. Version 1. Checksum: DFBE0AB499C998E3	FASTA	357	41,168
	10 20 30 40 50 60 MSKFWNDKIK EIEPYTPGEQ PKDKKYIKLN TNENPYPPSS KVIEKIKSMN LEDLKLYPDP 70 80 90 100 110 120 DVMELGKVIA EYFSNKINDK VTHKQVFIGN GSDEVLAFIF MTFFNAGDKV YYPDITYSFY 130 140 150 160 170 180 PVYADLFNVK EVKIPLNDSF EIEIQKYFGL DGHIIIANPN APTSIALKLD EIEEIVKNNP 190 200 210 220 230 240 NQLVIIDEAY VDFGAESAVK LINKYDNVLV VQTFSKSRFM AGIRLGYALG SENIIEGLNR 250 260 270 280 290 300 LKFSFNSYTI DRISIEAGIE SFKDDEYFEK TNAKIIQTRE KTVEKLKKLR FNVLNSSANF 310 320 330 340 350 IFISHNKVFA GDLYKQLKEN GVLVRYFAKD RIDNYLRITI GTDEEMGIFI EKLEEII

References

[1]

"Complete genome sequence of Leptotrichia buccalis type strain (C-1013-b)." Ivanova N., Gronow S., Lapidus A., Copeland A., Glavina del Rio T., Nolan M., Lucas S., Chen F., Tice H., Cheng J.-F., Saunders E., Bruce D., Goodwin L., Brettin T., Detter J.C., Han C., Pitluck S., Mikhailova N. , Pati A., Mavromatis K., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.-J., Jeffries C.C., Chain P., Rohde C., Goeker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.-P. Stand. Genomic Sci. 1:126-132(2009) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 14201 / DSM 1135 / JCM 12969 / NCTC 10249.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001685 Genomic DNA. Translation: ACV39125.1.
RefSeq	YP_003164116.1. NC_013192.1.
3D structure databases
ProteinModelPortal	C7NAE4.
ModBase	Search...
Protein-protein interaction databases
STRING	523794.Lebu_1235.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACV39125; ACV39125; Lebu_1235.
GeneID	8407941.
KEGG	lba:Lebu_1235.
PATRIC	22401797. VBILepBuc70646_1257.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0079.
HOGENOM	HOG000288510.
KO	K00817.
OMA	AHIFHGL.
ProtClustDB	PRK05387.
Enzyme and pathway databases
BioCyc	LBUC523794:GHCR-1262-MONOMER.
UniPathway	UPA00031; UER00012.
Family and domain databases
Gene3D	3.40.640.10. 1 hit. 3.90.1150.10. 1 hit.
HAMAP	MF_01023. HisC_aminotrans_2.
InterPro	IPR004839. Aminotransferase_I/II. IPR005861. HisP_aminotrans. IPR015424. PyrdxlP-dep_Trfase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
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

C7NAE4_LEPBD

Accession

Primary (citable) accession number: C7NAE4

Entry history

Integrated into UniProtKB/TrEMBL:	October 13, 2009
Last sequence update:	October 13, 2009
Last modified:	May 1, 2013
This is version 28 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)