Reviewed, UniProtKB/Swiss-Prot Q5QZ49 (HIS81_IDILO)

Names and origin

Protein names

Recommended name:
    Histidinol-phosphate aminotransferase 1
    EC=2.6.1.9
Alternative name(s):
    Imidazole acetol-phosphate transaminase 1

Gene names

Name:	hisC1
Ordered Locus Names:	IL1358

Organism

Idiomarina loihiensis [Complete proteome] [HAMAP]

Taxonomic identifier

135577 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Idiomarinaceae › Idiomarina

Protein attributes

Sequence length	367 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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.
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
Gene Ontology (GO)
Biological process	histidine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	1-aminocyclopropane-1-carboxylate synthase activity Inferred from electronic annotation. Source: InterPro 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
Molecule processing
	Chain	1 – 367	367	Histidinol-phosphate aminotransferase 1 HAMAP MF_01023		PRO_0000153373
Amino acid modifications
	Modified residue	229	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5QZ49-1 [UniParc]. Last modified January 4, 2005. Version 1. Checksum: A7B889BCCE38CEC1	FASTA	367	40,505
	10 20 30 40 50 60 MAEFNALELV NPGVKQLRPY QAGKPTSELQ RELGLQHVVK LASNENPLGL SEKVKTALEA 70 80 90 100 110 120 ELTDLVRYPD ANGYYLKSRL AELNEVGTQQ ITLGNGSNDV LEILARTFVS DKDEVIFSQH 130 140 150 160 170 180 AFVVYPLVTQ AIGAKPVAVP AVDYGHDLDG MAKAVTDKTK MIFIANPNNP TGTFLSTSAL 190 200 210 220 230 240 KSFLDKIPQH IIVVLDEAYY EYVPEDQRAP SVEWIKEYPN LVVSRTFSKA YGLAGLRAGY 250 260 270 280 290 300 AVSHESVADV LNRIRQPFNM NSLSLKAAEV VLDDHAYLQK AVELNAQGMQ LLTEFCEESG 310 320 330 340 350 360 LNYIPSYGNF LTIEVGPGAE KLYDELLHEG VIVRPVGGYE LPNHLRVSIG LPEENQAFIK AMKKLRG

References

[1]

"Genome sequence of the deep-sea gamma-proteobacterium Idiomarina loihiensis reveals amino acid fermentation as a source of carbon and energy." Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y., Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S., Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S., Denery J. , Aizawa S., Shibata S., Malahoff A., Alam M. Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004) [PubMed: 15596722] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: L2-TR / ATCC BAA-735 / DSM 15497.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE017340 Genomic DNA. Translation: AAV82198.1.
RefSeq	YP_155747.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3173565.
GenomeReviews	Gene locus IL1358 in contig AE017340_GR.
KEGG	ilo:IL1358.
NMPDR	fig|283942.3.peg.1610.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q5QZ49.
OMA	ENTLIVI.
Enzyme and pathway databases
BioCyc	ILOI283942:IL1358-MON.
BRENDA	2.6.1.9. 280818.
Family and domain databases
HAMAP	MF_01023. [Tree]
InterPro	IPR001176. ACC_synthase. IPR001917. Aminotrans_II_pyridoxalP_BS. IPR004839. Aminotransferase_I/II. IPR005861. HisP_aminotrans. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
Pfam	PF00155. Aminotran_1_2. 1 hit. [Graphical view]
PRINTS	PR00753. ACCSYNTHASE.
TIGRFAMs	TIGR01141. hisC. 1 hit.
PROSITE	PS00599. AA_TRANSFER_CLASS_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HIS81_IDILO

Accession

Primary (citable) accession number: Q5QZ49

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2006
Last sequence update:	January 4, 2005
Last modified:	November 3, 2009
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)