Q9S5G5 (HIS7_ECO57) 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:	Z3184, ECs2823

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	355 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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.
Sequence caution	The sequence AAG57081.1 differs from that shown. Reason: Erroneous initiation. The sequence BAB36246.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis
Cellular component	Cytoplasm
Molecular function	Hydrolase Lyase
Technical term	3D-structure 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 – 355

355

Histidine biosynthesis bifunctional protein hisB HAMAP MF_01022

PRO_0000158208

Regions

Region

1 – 166

166

Histidinol-phosphatase HAMAP MF_01022

Region

167 – 355

189

Imidazoleglycerol-phosphate dehydratase HAMAP MF_01022

Secondary structure

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355

Helix Strand Turn

Details...

Beta strand

4 – 8

5

Turn

12 – 14

3

Helix

27 – 29

3

Helix

36 – 45

10

Beta strand

48 – 55

8

Turn

57 – 60

4

Helix

66 – 82

17

Beta strand

87 – 93

7

Helix

97 – 99

3

Beta strand

102 – 104

3

Helix

109 – 114

6

Helix

122 – 124

3

Beta strand

126 – 131

6

Helix

132 – 141

10

Beta strand

143 – 147

5

Turn

150 – 152

3

Helix

155 – 161

7

Sequences

	Sequence		Length	Mass (Da)
	Q9S5G5 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 91229A10D62A4EE8	FASTA	355	40,290
	10 20 30 40 50 60 MSQKYLFIDR DGTLISEPPS DFQVDRFDKL AFEPGVIPQL LKLQKAGYKL VMITNQDGLG 70 80 90 100 110 120 TQSFPQADFD GPHNLMMQIF TSQGVQFDEV LICPHLPADE CDCRKPKVKL VERYLAEQAM 130 140 150 160 170 180 DRANSYVIGD RATDIQLAEN MGINGLRYDR ETLNWPMIGE QLTRRDRYAH VVRNTKETQI 190 200 210 220 230 240 DVQVWLDREG GSKINTGVGF FDHMLDQIAT HGGFRMEINV KGDLYIDDHH TVEDTGLALG 250 260 270 280 290 300 EALKIALGDK RGICRFGFVL PMDECLARCA LDISGRPHLE YKAEFTYQRV GDLSTEMIEH 310 320 330 340 350 FFRSLSYTMG VTLHLKTKGK NDHHRVESLF KAFGRTLRQA IRVEGDTLPS SKGVL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of the genes responsible for the O-antigen synthesis in enterohaemorrhagic Escherichia coli O157." Shimizu T., Yamasaki S., Tsukamoto T., Takeda Y. Microb. Pathog. 26:235-247(1999) [PubMed: 10222209] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: O157:H- / 184 / EHEC.
[2]	"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R. Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[3]	"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB008676 Genomic DNA. Translation: BAA77743.1.
AE005174 Genomic DNA. Translation: AAG57081.1. Different initiation.
BA000007 Genomic DNA. Translation: BAB36246.1. Different initiation.

PIR

E85827.
G90981.

RefSeq

NP_288527.2. NC_002655.2.
NP_310850.2. NC_002695.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2FPR	X-ray	1.70	A/B	2-165	[»]
2FPS	X-ray	2.20	A/B	2-165	[»]
2FPU	X-ray	1.80	A/B	2-165	[»]
2FPW	X-ray	1.75	A/B	2-165	[»]
2FPX	X-ray	1.80	A/B	2-165	[»]

ProteinModelPortal

Q9S5G5.

SMR

Q9S5G5. Positions 3-165.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000027077; EBESCP00000025970; EBESCG00000026129.
EBESCT00000055491; EBESCP00000053319; EBESCG00000054539.

GeneID

914091.
962080.

GenomeReviews

Gene locus Z3184 in contig AE005174_GR.
Gene locus ECs2823 in contig BA000007_GR.

KEGG

ece:Z3184.
ecs:ECs2823.

PATRIC

18355034. VBIEscCol44059_2718.

Organism-specific databases

CMR

Search...

Phylogenomic databases

GeneTree

EBGT00050000010149.

HOGENOM

HBG289010.

OMA

EMVPHFF.

ProtClustDB

PRK05446.

Enzyme and pathway databases

BioCyc

ECOL83334:ECS2823-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_ECO57

Accession

Primary (citable) accession number: Q9S5G5
Secondary accession number(s): Q8X8T1

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 24, 2002
Last sequence update:	May 1, 2000
Last modified:	January 25, 2012
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program