Reviewed, UniProtKB/Swiss-Prot Q4UU42 (HIS7_XANC8)

Names and origin

Protein names

Recommended name:
    Histidine biosynthesis bifunctional protein hisB
Including the following 2 domains:
    1- Recommended name:
            Histidinol-phosphatase
              EC=3.1.3.15
    2- Recommended name:
            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.
Sequence processing	The displayed sequence is not processed.
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.
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: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	histidinol-phosphatase activity Inferred from electronic annotation. Source: HAMAP imidazoleglycerol-phosphate dehydratase activity Inferred from electronic annotation. Source: HAMAP
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)
	Q4UU42-1 [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].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000050 Genomic DNA. Translation: AAY49431.1.
RefSeq	YP_243451.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3380915.
GenomeReviews	Gene locus XC_2378 in contig CP000050_GR.
KEGG	xcb:XC_2378.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q4UU42.
OMA	Q4UU42. MVSNQDG.
Enzyme and pathway databases
BioCyc	XCAM314565:XC_2378-MON.
Family and domain databases
HAMAP	MF_01022. [Tree]
InterPro	IPR006549. HAD-SF_hydro_IIIA. IPR005954. HisB_N. IPR006543. Histidinol-phos. IPR000807. Imidazole_glycer-P_deHydtase. IPR013954. PNK3P_central-region. [Graphical view]
PANTHER	PTHR23133:SF2. Imidazole-GPD. 1 hit.
Pfam	PF00475. IGPD. 1 hit. PF08645. PNK3P. 1 hit. [Graphical view]
ProDom	PD002282. IGPD. 1 hit. [Graphical view] [Entries sharing at least one domain]
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:	June 16, 2009
This is version 24 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)