P71703 (INO1_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Inositol-3-phosphate synthase
Short name=IPS
EC=5.5.1.4

Alternative name(s):
Myo-inositol 1-phosphate synthase
Short name=MI-1-P synthase
Short name=MIP synthase

Gene names

Name:	ino1
Ordered Locus Names:	Rv0046c, MT0052
ORF Names:	MTCY21D4.09c

Organism

Mycobacterium tuberculosis [Reference proteome] [HAMAP]

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	367 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the conversion of glucose 6-phosphate to 1D-myo-inositol 3-phosphate By similarity.
Catalytic activity	D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate.
Post-translational modification	Pupylated at Lys-73 by the prokaryotic ubiquitin-like protein Pup, which leads to its degradation by the proteasome. Ref.3
Miscellaneous	Was identified as a natural substrate of the M.tuberculosis proteasome.
Sequence similarities	Belongs to the myo-inositol 1-phosphate synthase family.

Ontologies

Keywords
Biological process	Inositol biosynthesis
Molecular function	Isomerase
PTM	Isopeptide bond Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	inositol biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW mycothiol biosynthetic process Traceable author statement. Source: Reactome pathogenesis Inferred from mutant phenotype PubMed 14763976. Source: MTBBASE phospholipid biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytosol Traceable author statement. Source: Reactome
Molecular_function	inositol-3-phosphate synthase activity Inferred from mutant phenotype PubMed 10448034. Source: MTBBASE zinc ion binding Inferred from direct assay PubMed 12005437. Source: MTBBASE
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 367

367

Inositol-3-phosphate synthase

PRO_0000195203

Amino acid modifications

Cross-link

73

Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)

Experimental info

Sequence conflict

190

1

R → G in AAK44274. Ref.2

Secondary structure

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367

Helix Strand Turn

Details...

Beta strand

16 – 21

6

Helix

25 – 36

12

Turn

37 – 39

3

Beta strand

52 – 54

3

Helix

59 – 61

3

Beta strand

62 – 69

8

Turn

72 – 76

5

Helix

79 – 82

4

Helix

114 – 117

4

Helix

130 – 136

7

Beta strand

140 – 144

5

Helix

151 – 164

14

Beta strand

167 – 170

4

Helix

180 – 189

10

Beta strand

192 – 198

7

Helix

204 – 217

14

Beta strand

221 – 231

11

Helix

234 – 240

7

Beta strand

272 – 276

5

Helix

278 – 280

3

Beta strand

283 – 294

12

Helix

295 – 297

3

Beta strand

298 – 309

12

Helix

312 – 330

19

Helix

338 – 344

7

Beta strand

345 – 347

3

Helix

354 – 366

13

Sequences

	Sequence		Length	Mass (Da)
	P71703 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 3976AA08452183F9	FASTA	367	40,094
	10 20 30 40 50 60 MSEHQSLPAP EASTEVRVAI VGVGNCASSL VQGVEYYYNA DDTSTVPGLM HVRFGPYHVR 70 80 90 100 110 120 DVKFVAAFDV DAKKVGFDLS DAIFASENNT IKIADVAPTN VIVQRGPTLD GIGKYYADTI 130 140 150 160 170 180 ELSDAEPVDV VQALKEAKVD VLVSYLPVGS EEADKFYAQC AIDAGVAFVN ALPVFIASDP 190 200 210 220 230 240 VWAKKFTDAR VPIVGDDIKS QVGATITHRV LAKLFEDRGV QLDRTMQLNV GGNMDFLNML 250 260 270 280 290 300 ERERLESKKI SKTQAVTSNL KREFKTKDVH IGPSDHVGWL DDRKWAYVRL EGRAFGDVPL 310 320 330 340 350 360 NLEYKLEVWD SPNSAGVIID AVRAAKIAKD RGIGGPVIPA SAYLMKSPPE QLPDDIARAQ LEEFIIG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G. Nature 393:537-544(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[2]	"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
[3]	"Prokayrotic ubiquitin-like protein (Pup) proteome of Mycobacterium tuberculosis." Festa R.A., McAllister F., Pearce M.J., Mintseris J., Burns K.E., Gygi S.P., Darwin K.H. PLoS ONE 5:E8589-E8589(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEASOME SUBSTRATE, PUPYLATION AT LYS-73, IDENTIFICATION BY MASS SPECTROMETRY. Strain: ATCC 25618 / H37Rv.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE000516 Genomic DNA. Translation: AAK44274.1.
AL123456 Genomic DNA. Translation: CCP42768.1.

PIR

F70912.

RefSeq

NP_214560.1. NC_000962.3.
NP_334460.1. NC_002755.2.
YP_006513360.1. NC_018143.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GR0	X-ray	1.95	A	1-367	[»]

ProteinModelPortal

P71703.

SMR

P71703. Positions 14-367.

ModBase

Search...

Protein-protein interaction databases

STRING

83332.Rv0046c.

Proteomic databases

PRIDE

P71703.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAK44274; AAK44274; MT0052.

GeneID

13316024.
887028.
922655.

KEGG

mtc:MT0052.
mtu:Rv0046c.

PATRIC

18121837. VBIMycTub22151_0053.

Organism-specific databases

TubercuList

Rv0046c.

Phylogenomic databases

eggNOG

COG1260.

HOGENOM

HOG000224236.

KO

K01858.

OMA

YTMKHPP.

ProtClustDB

CLSK871751.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-5061.

Reactome

REACT_27295. Mycobacterium tuberculosis biological processes.

Family and domain databases

Gene3D

3.40.50.720. 2 hits.

InterPro

IPR002587. Myo-inos-1-P_Synthase.
IPR017815. Myo-inos-1-P_Synthase_actino.
IPR013021. Myo-inos-1-P_Synthase_GAPDH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]

PANTHER

PTHR11510. PTHR11510. 1 hit.

Pfam

PF01658. Inos-1-P_synth. 1 hit.
PF07994. NAD_binding_5. 1 hit.
[Graphical view]

PIRSF

PIRSF015578. Myoinos-ppht_syn. 1 hit.

TIGRFAMs

TIGR03450. mycothiol_INO1. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P71703.

Entry information

Entry name

INO1_MYCTU

Accession

Primary (citable) accession number: P71703
Secondary accession number(s): L0T457

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2001
Last sequence update:	February 1, 1997
Last modified:	May 29, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program