P44327 (HIS7_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histidine biosynthesis bifunctional protein hisB

Including the following 2 domains:

1. Histidinol-phosphatase
   EC=3.1.3.15
2. Imidazoleglycerol-phosphate dehydratase
   Short name=IGPD
   EC=4.2.1.19

Gene names

Name:	hisB
Ordered Locus Names:	HI_0471

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	362 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O. HAMAP MF_01022 L-histidinol phosphate + H2O = L-histidinol + phosphate. HAMAP MF_01022
Pathway	Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9. HAMAP MF_01022 Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
Subcellular location	Cytoplasm By similarity HAMAP MF_01022.
Sequence similarities	In the N-terminal section; belongs to the histidinol-phosphatase family. In the C-terminal section; belongs to the imidazoleglycerol-phosphate dehydratase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis
Cellular component	Cytoplasm
Molecular function	Hydrolase Lyase
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological process	histidine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	histidinol-phosphatase activity Inferred from electronic annotation. Source: EC imidazoleglycerol-phosphate dehydratase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 362	362	Histidine biosynthesis bifunctional protein hisB HAMAP MF_01022		PRO_0000158210
Regions
	Region	1 – 173	173	Histidinol-phosphatase HAMAP MF_01022
	Region	174 – 362	189	Imidazoleglycerol-phosphate dehydratase HAMAP MF_01022

Sequences

	Sequence		Length	Mass (Da)
	P44327 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: A031E606EAD2EAE5	FASTA	362	41,162
	10 20 30 40 50 60 MQPTLFIDRD GTLIDEPKTD FQIDSLEKLK LEPKVIPALL RLKAKYRFVI VSNQDGLGTD 70 80 90 100 110 120 AFPQTDFDKP HNVMMALFES QGITFDEVLI CPHKPEENCL CRKPKIKLLD HYIRKNLFDI 130 140 150 160 170 180 DRSFVIGDRE TDVQLAENLG IRAIQYDPQK MNWDLIAEKL LGETVTNCGK RPPRFAEVIR 190 200 210 220 230 240 QTKETDIKVQ VWLDEAGVNE IKTGVGFFDH MLDQIATHGG FRMNVQCKGD LWIDEHHTVE 250 260 270 280 290 300 DTALALGQAL KQAVGDKRGI ARFGFVLPMD ECKAECALDL SGRPWIKFNA CFKRDKVGDF 310 320 330 340 350 360 STELTEHFFQ SLAFSMLATL HLNVTGNNDH HKIESLFKAF GRTLRQAIRI EGNEMPSSKG VL

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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L42023 Genomic DNA. Translation: AAC22130.1.
PIR	F64070.
RefSeq	NP_438632.1. NC_000907.1.
3D structure databases
ProteinModelPortal	P44327.
SMR	P44327. Positions 2-160.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	949564.
GenomeReviews	Gene locus HI_0471 in contig L42023_GR.
KEGG	hin:HI0471.
NMPDR	fig|71421.1.peg.445.
PATRIC	20189497. VBIHaeInf48452_0491.
TIGR	HI_0471.
Phylogenomic databases
HOGENOM	HBG289010.
OMA	EMVPHFF.
PhylomeDB	P44327.
ProtClustDB	PRK05446.
Enzyme and pathway databases
BioCyc	HINF71421:HI_0471-MONOMER.
Family and domain databases
HAMAP	MF_01022. Bifunc_HisB. [Tree]
InterPro	IPR023214. HAD-like_dom. IPR006549. HAD-SF_hydro_IIIA. IPR020566. His_synth_bifunc_HisB. IPR005954. HisB_N. IPR006543. Histidinol-phos. IPR000807. ImidazoleglycerolP_deHydtase. IPR020565. ImidazoleglycerP_deHydtase_CS. IPR020568. Ribosomal_S5_D2-typ_fold. [Graphical view]
Gene3D	G3DSA:3.40.50.1000. HAD-like_dom. 1 hit.
KO	K01089.
PANTHER	PTHR23133:SF2. Imidazole-GPD. 1 hit.
Pfam	PF00475. IGPD. 1 hit. [Graphical view]
SUPFAM	SSF56784. HAD-like_dom. 1 hit. SSF54211. Ribosomal_S5_D2-typ_fold. 2 hits.
TIGRFAMs	TIGR01662. HAD-SF-IIIA. 1 hit. TIGR01261. HisB_Nterm. 1 hit. TIGR01656. Histidinol-ppas. 1 hit.
PROSITE	PS00954. IGP_DEHYDRATASE_1. 1 hit. PS00955. IGP_DEHYDRATASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HIS7_HAEIN

Accession

Primary (citable) accession number: P44327

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	January 25, 2012
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program