Q5LNM6 (HIS8_SILPO) 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:	SPO3177

Organism

Silicibacter pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) [Complete proteome] [HAMAP]

Taxonomic identifier

246200 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Ruegeria

Protein attributes

Sequence length	361 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.
Sequence caution	The sequence AAV96412.1 differs from that shown. Reason: Erroneous initiation.

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 – 361	361	Histidinol-phosphate aminotransferase HAMAP MF_01023		PRO_0000153450
Amino acid modifications
	Modified residue	218	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5LNM6 [UniParc]. Last modified January 10, 2006. Version 2. Checksum: E5C775B77DD266C6	FASTA	361	38,782
	10 20 30 40 50 60 MNQFTPQPGI MDIALYQGGK AHVDGVANVI KLSSNENPLG PSPAAVEAIR ATAAQAHRYP 70 80 90 100 110 120 STDHAELRAA IGAVHGLDPD RIICGVGSDE VLQFVAQAYT GPGDEVIHTE HGFSMYPILA 130 140 150 160 170 180 RMAGATPVQV PERQRVVDVD AILAAVNDRT RLVFLANPAN PTGTMISEAE VTRLADGLPG 190 200 210 220 230 240 HVLLVLDGAY AEFVEGFDGG AALVSARDNV IMTRTFSKIY GLGGLRIGWG YAPREIIDVL 250 260 270 280 290 300 NRIRQPFNLS TMQLAAAEAA VRDQDWVARC RDQNTTWRTW LAARLAELGV PSDVSCANFI 310 320 330 340 350 360 LARFADQGEA EACDLFLQSR GLIVRRVAGY NLPQALRITV GDEAGCRAVV DAVRAFKEAR A

References

[1]

"Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine environment." Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B., Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.M., Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M. , Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q., Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N. Nature 432:910-913(2004) [PubMed: 15602564] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700808 / DSM 15171 / DSS-3.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000031 Genomic DNA. Translation: AAV96412.1. Different initiation.
RefSeq	YP_168380.1. NC_003911.11.
3D structure databases
ProteinModelPortal	Q5LNM6.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3195649.
GenomeReviews	Gene locus SPO3177 in contig CP000031_GR.
KEGG	sil:SPO3177.
NMPDR	fig|246200.3.peg.3550.
PATRIC	23379801. VBIRuePom114501_3244.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG646350.
OMA	YPSTDHA.
ProtClustDB	PRK02731.
Enzyme and pathway databases
BioCyc	RPOM246200:SPO_3177-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_SILPO

Accession

Primary (citable) accession number: Q5LNM6

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2006
Last sequence update:	January 10, 2006
Last modified:	January 25, 2012
This is version 47 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program