Q4UU42 (HIS7_XANC8) 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:	XC_2378

Organism

Xanthomonas campestris pv. campestris (strain 8004) [Complete proteome] [HAMAP]

Taxonomic identifier

314565 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xanthomonas

Protein attributes

Sequence length	375 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 – 375	375	Histidine biosynthesis bifunctional protein hisB HAMAP MF_01022		PRO_1000063451
Regions
	Region	1 – 168	168	Histidinol-phosphatase HAMAP MF_01022
	Region	169 – 375	207	Imidazoleglycerol-phosphate dehydratase HAMAP MF_01022

Sequences

	Sequence		Length	Mass (Da)
	Q4UU42 [UniParc]. Last modified July 5, 2005. Version 1. Checksum: 758A9F43F0F5AF72	FASTA	375	41,812
	10 20 30 40 50 60 MTPILFVDRD GTLITEPADF QIDAYEKLRF VDGVIPAMLK LRDAGYQFVI VSNQDGLGSE 70 80 90 100 110 120 SYPQASFDGP NNLMLQIFAS QGIVFREVLI DCSWPADNAP TRKPGVGLMV PYLQDRTIDW 130 140 150 160 170 180 SRSAMVGDRI TDIQFAQNLN IRGFQLRTEQ FGGDWDWAGI AHELADAPRR AVVQRNTKET 190 200 210 220 230 240 RIRVELDLDR VAEPHTATGL PFFDHMLEQI GKHGGFALDI RAEGDLHIDE HHTIEDTGLA 250 260 270 280 290 300 LGQALREALG DKRGIGRYGF DPDDSPWRVA GDTTQHGFTL PMDETIASAA LDFSGRPYFV 310 320 330 340 350 360 FDGDFKRERV GDMPTELVPH FFRSVCDASG LNLHLHVRGE NDHHKVEGCF KALARALRQA 370 IRREGTALPS TKGAL

References

[1]

"Comparative and functional genomic analyses of the pathogenicity of phytopathogen Xanthomonas campestris pv. campestris." Qian W., Jia Y., Ren S.-X., He Y.-Q., Feng J.-X., Lu L.-F., Sun Q., Ying G., Tang D.-J., Tang H., Wu W., Hao P., Wang L., Jiang B.-L., Zeng S., Gu W.-Y., Lu G., Rong L. , Tian Y., Yao Z., Fu G., Chen B., Fang R., Qiang B., Chen Z., Zhao G.-P., Tang J.-L., He C. Genome Res. 15:757-767(2005) [PubMed: 15899963] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 8004.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000050 Genomic DNA. Translation: AAY49431.1.
RefSeq	YP_243451.1. NC_007086.1.
3D structure databases
HSSP	HSSP built from PDB template 2F1D based on UniProtKB P34047.
ProteinModelPortal	Q4UU42.
ModBase	Search...
Protein-protein interaction databases
STRING	Q4UU42.
Proteomic databases
PRIDE	Q4UU42.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3380915.
GenomeReviews	Gene locus XC_2378 in contig CP000050_GR.
KEGG	xcb:XC_2378.
PATRIC	24066322. VBIXanCam24967_2547.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0131.
HOGENOM	HBG289010.
OMA	EMVPHFF.
PhylomeDB	Q4UU42.
ProtClustDB	PRK05446.
Enzyme and pathway databases
BioCyc	XCAM314565:XC_2378-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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HIS7_XANC8

Accession

Primary (citable) accession number: Q4UU42

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	July 5, 2005
Last modified:	January 25, 2012
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program