Q9PM74 (HIS4_CAMJE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase
EC=5.3.1.16

Alternative name(s):
Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase

Gene names

Name:	hisA
Ordered Locus Names:	Cj1601

Organism

Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168) [Reference proteome] [HAMAP]

Taxonomic identifier

192222 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › delta/epsilon subdivisions › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter › Campylobacter jejuni › Campylobacter jejuni subsp. jejuni

Protein attributes

Sequence length	243 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide = 5-((5-phospho-1-deoxyribulos-1-ylamino)methylideneamino)-1-(5-phosphoribosyl)imidazole-4-carboxamide. HAMAP-Rule MF_01014
Pathway	Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9. HAMAP-Rule MF_01014
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the HisA/HisF family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis
Cellular component	Cytoplasm
Molecular function	Isomerase
Technical term	3D-structure Complete proteome Reference proteome
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	1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase 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 – 243

243

1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase HAMAP-Rule MF_01014

PRO_0000141993

Sites

Active site

9

1

Proton acceptor By similarity

Active site

131

1

Proton donor By similarity

Secondary structure

1

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243

Helix Strand Turn

Details...

Beta strand

3 – 11

9

Beta strand

14 – 19

6

Beta strand

21 – 23

3

Beta strand

25 – 28

4

Helix

33 – 43

11

Beta strand

47 – 52

6

Helix

53 – 57

5

Helix

59 – 61

3

Helix

64 – 73

10

Beta strand

76 – 83

8

Helix

87 – 95

9

Beta strand

99 – 103

5

Turn

105 – 109

5

Helix

111 – 121

11

Turn

123 – 125

3

Beta strand

126 – 140

15

Helix

153 – 161

9

Turn

162 – 164

3

Beta strand

167 – 172

6

Helix

184 – 193

10

Beta strand

197 – 203

7

Helix

208 – 213

6

Turn

214 – 217

4

Beta strand

219 – 223

5

Helix

225 – 228

4

Helix

234 – 241

8

Sequences

	Sequence		Length	Mass (Da)
	Q9PM74 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 23AE7D77A2ECD9A9	FASTA	243	26,684
	10 20 30 40 50 60 MTQIIPALDL IDGEVVRLVK GDYEQKKVYK YNPLKKFKEY EKAGAKELHL VDLTGAKDPS 70 80 90 100 110 120 KRQFALIEKL AKEVSVNLQV GGGIRSKEEV KALLDCGVKR VVIGSMAIKD ATLCLEILKE 130 140 150 160 170 180 FGSEAIVLAL DTILKEDYVV AVNAWQEASD KKLMEVLDFY SNKGLKHILC TDISKDGTMQ 190 200 210 220 230 240 GVNVRLYKLI HEIFPNICIQ ASGGVASLKD LENLKGICSG VIVGKALLDG VFSVEEGIRC LAN

References

[1]

"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences." Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. , van Vliet A.H.M., Whitehead S., Barrell B.G. Nature 403:665-668(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 11168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AL111168 Genomic DNA. Translation: CAL35698.1.

PIR

G81255.

RefSeq

YP_002344970.1. NC_002163.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4GJ1	X-ray	2.15	A	1-243	[»]

ProteinModelPortal

Q9PM74.

ModBase

Search...

Protein-protein interaction databases

STRING

192222.Cj1601.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAL35698; CAL35698; Cj1601.

GeneID

904505.

KEGG

cje:Cj1601.

PATRIC

20060162. VBICamJej33762_1577.

Phylogenomic databases

eggNOG

COG0106.

HOGENOM

HOG000224614.

KO

K01814.

OMA

DGHCVRL.

ProtClustDB

PRK00748.

Enzyme and pathway databases

BioCyc

CJEJ192222:GJTS-1560-MONOMER.

UniPathway

UPA00031; UER00009.

Family and domain databases

Gene3D

3.20.20.70. 1 hit.

HAMAP

MF_01014. HisA.

InterPro

IPR013785. Aldolase_TIM.
IPR006062. His_biosynth.
IPR006063. HisA.
IPR023016. Isoase_HisA.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]

Pfam

PF00977. His_biosynth. 1 hit.
[Graphical view]

SUPFAM

SSF51366. RibP_bind_barrel. 1 hit.

TIGRFAMs

TIGR00007. TIGR00007. 1 hit.

ProtoNet

Search...

Entry information

Entry name

HIS4_CAMJE

Accession

Primary (citable) accession number: Q9PM74
Secondary accession number(s): Q0P827

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2002
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
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