P44423 (HIS81_HAEIN) Reviewed, UniProtKB/Swiss-Prot

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
Synonyms:	hisC
Ordered Locus Names:	HI_0470

Organism

Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)

Taxonomic identifier

71421 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length	367 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.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	Complete proteome Reference 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 – 367	367	Histidinol-phosphate aminotransferase 1 HAMAP MF_01023		PRO_0000153368
Amino acid modifications
	Modified residue	226	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P44423 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 8594237F1C530465	FASTA	367	40,794
	10 20 30 40 50 60 MNDYNSHILQ WKKTIMTITT LSRQNIQALT PYQSARKLGG NGTIWLNANE YPTSPEFQLS 70 80 90 100 110 120 GKDLNRYPEP QPQRVVQAYA NYAGVSTENV LVTRGGDEGI ELIIHTFCEP KQDAILFCPP 130 140 150 160 170 180 TYGMYAVSAE TAGVLSKTVP LTDDFQLNLP EIKNHLNDVK VVFVCSPNNP TGNLLKQSDI 190 200 210 220 230 240 LDLLQITAGK AIVVVDEAYI EFCPEASVIN LLKNYPHLAI IRTLSKAFAL AGLRCGFVLA 250 260 270 280 290 300 NPELIDILSK VIAPYPIPVP SADLAEQALR PSNIATVQAL TQELLSNRQW LAKALLVLHQ 310 320 330 340 350 360 VEKVYESEAN YLLIKCQNGQ AVFKALWEQG IILRDQNKTL HLQNCIRITV GTRNECEKVV EAIKEVK

References

[1]

"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed: 7542800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L42023 Genomic DNA. Translation: AAC22129.1.
PIR	E64070.
RefSeq	NP_438631.1. NC_000907.1.
3D structure databases
ProteinModelPortal	P44423.
SMR	P44423. Positions 16-364.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	949558.
GenomeReviews	Gene locus HI_0470 in contig L42023_GR.
KEGG	hin:HI0470.
NMPDR	fig|71421.1.peg.444.
PATRIC	20189495. VBIHaeInf48452_0490.
TIGR	HI_0470.
Phylogenomic databases
HOGENOM	HBG646350.
OMA	RDQRAVP.
PhylomeDB	P44423.
ProtClustDB	PRK01688.
Enzyme and pathway databases
BioCyc	HINF71421:HI_0470-MONOMER.
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

HIS81_HAEIN

Accession

Primary (citable) accession number: P44423

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	January 25, 2012
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program