Q47XB6 (HIS7_COLP3) 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:	CPS_3892

Organism

Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio psychroerythus) [Complete proteome] [HAMAP]

Taxonomic identifier

167879 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Colwelliaceae › Colwellia

Protein attributes

Sequence length	361 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
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 – 361	361	Histidine biosynthesis bifunctional protein hisB HAMAP MF_01022		PRO_0000319738
Regions
	Region	1 – 172	172	Histidinol-phosphatase HAMAP MF_01022
	Region	173 – 361	189	Imidazoleglycerol-phosphate dehydratase HAMAP MF_01022

Sequences

	Sequence		Length	Mass (Da)
	Q47XB6 [UniParc]. Last modified September 13, 2005. Version 1. Checksum: 0DAD638A63B8A9F1	FASTA	361	39,901
	10 20 30 40 50 60 MSNTQEKILF IDRDGTLVEE PAIDKQLDTL EKLVFEPNVI AELLKLQAKG FKLVMVSNQD 70 80 90 100 110 120 GLGTNSFPQA DFDLPHNKMM DLFSSQGVHF QDVLLCPHFD EDNCNCRKPK LGLVSEYLQQ 130 140 150 160 170 180 GRVDFANSFV IGDRETDMGL AANMGIVGIK YDPETLNWAQ VSEQIITQLE QPRIATVTRT 190 200 210 220 230 240 TKETDITVTV NLDKAGESSI DTGLGFFDHM LDQISTHGGF SLQCHVSGDY HIDEHHSVED 250 260 270 280 290 300 TALALGQALK QALGNKRGIN RFGFTIPMDE CRAECAIDLS GRPWLEFDAD FTSANVGTMS 310 320 330 340 350 360 TQMVPHFFRS LADSMLITLH LSTSKGNCHH QVESLFKVFG RALGQAIKVD GDAMPSSKGT L

References

[1]

"The psychrophilic lifestyle as revealed by the genome sequence of Colwellia psychrerythraea 34H through genomic and proteomic analyses." Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X., Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M., Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A., Zhou L., Davidsen T.M. , Wu M., Huston A.L., Lewis M., Weaver B., Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M. Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005) [PubMed: 16043709] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 34H / ATCC BAA-681.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000083 Genomic DNA. Translation: AAZ28659.1.
RefSeq	YP_270554.1. NC_003910.7.
3D structure databases
HSSP	HSSP built from PDB template 2F1D based on UniProtKB P34047.
ProteinModelPortal	Q47XB6.
SMR	Q47XB6. Positions 6-165.
ModBase	Search...
Protein-protein interaction databases
STRING	Q47XB6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3522920.
GenomeReviews	Gene locus CPS_3892 in contig CP000083_GR.
KEGG	cps:CPS_3892.
NMPDR	fig|167879.3.peg.3532.
PATRIC	21470681. VBIColPsy94388_3529.
TIGR	CPS_3892.
Phylogenomic databases
eggNOG	COG0131.
HOGENOM	HBG289010.
OMA	EMVPHFF.
ProtClustDB	PRK05446.
Enzyme and pathway databases
BioCyc	CPSY167879:CPS_3892-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. IPR013954. PNK3P. 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. PF08645. PNK3P. 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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HIS7_COLP3

Accession

Primary (citable) accession number: Q47XB6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 26, 2008
Last sequence update:	September 13, 2005
Last modified:	January 25, 2012
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program