Myo-inositol-1-phosphate synthase (Ino1) - Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)

Preferred order of sections

Names and origin

Protein names

Submitted name:
Myo-inositol-1-phosphate synthase (Ino1) EMBL AAB89456.1

Gene names

Ordered Locus Names:

AF_1794

Organism

Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) [Reference proteome] [HAMAP] EMBL AAB89456.1

Taxonomic identifier

224325 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Archaeoglobi › Archaeoglobales › Archaeoglobaceae › Archaeoglobus ›

Protein attributes

Sequence length	392 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Ligand	NAD PDB 1U1I Nucleotide-binding PDB 1U1I
Technical term	3D-structure PDB 3QVS PDB 1U1I PDB 3QVT PDB 3QVW PDB 3QVX PDB 3QW2 Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	inositol biosynthetic process Inferred from electronic annotation. Source: InterPro phospholipid biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular_function	inositol-3-phosphate synthase activity Inferred from electronic annotation. Source: InterPro nucleotide binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Regions

Nucleotide binding

10 – 12

3

NAD PDB 1U1I

Nucleotide binding

57 – 59

3

NAD PDB 1U1I

Nucleotide binding

148 – 150

3

NAD PDB 1U1I

Sites

Binding site

99

1

NAD; via carbonyl oxygen PDB 1U1I

Binding site

185

1

NAD PDB 1U1I

Binding site

199

1

NAD PDB 1U1I

Binding site

228

1

NAD PDB 1U1I

Binding site

261

1

NAD PDB 1U1I

Binding site

274

1

NAD PDB 1U1I

Binding site

332

1

NAD PDB 1U1I

Sequences

Sequence

Length

Mass (Da)

Tools

O28480 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 387B0AFA946EBFDB
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FASTA

392

43,713

        10         20         30         40         50         60 
MKVWLVGAYG IVSTTAMVGA RAIERGIAPK IGLVSELPHF EGIEKYAPFS FEFGGHEIRL 

        70         80         90        100        110        120 
LSNAYEAAKE HWELNRHFDR EILEAVKSDL EGIVARKGTA LNCGSGIKEL GDIKTLEGEG 

       130        140        150        160        170        180 
LSLAEMVSRI EEDIKSFADD ETVVINVAST EPLPNYSEEY HGSLEGFERM IDEDRKEYAS 

       190        200        210        220        230        240 
ASMLYAYAAL KLGLPYANFT PSPGSAIPAL KELAEKKGVP HAGNDGKTGE TLVKTTLAPM 

       250        260        270        280        290        300 
FAYRNMEVVG WMSYNILGDY DGKVLSARDN KESKVLSKDK VLEKMLGYSP YSITEIQYFP 

       310        320        330        340        350        360 
SLVDNKTAFD FVHFKGFLGK LMKFYFIWDA IDAIVAAPLI LDIARFLLFA KKKGVKGVVK 

       370        380        390 
EMAFFFKSPM DTNVINTHEQ FVVLKEWYSN LK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus." Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G. Venter J.C. Nature 390:364-370(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.
[2]	"Reaching for mechanistic consensus across life kingdoms: structure and insights into catalysis of the myo-inositol-1-phosphate synthase (mIPS) from Archaeoglobus fulgidus." Stieglitz K.A., Yang H., Roberts M.F., Stec B. Biochemistry 44:213-224(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH NAD.
[3]	"Atomic crowding drives the catalysis of myo-inositol phosphate synthase, as deduced from a crystal structure of a trapped catalytic intermediate." Neelon K., Roberts M.F., Stec B. Submitted (FEB-2011) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE000782 Genomic DNA. Translation: AAB89456.1.

PIR

A69474.

RefSeq

NP_070622.1. NC_000917.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1U1I	X-ray	1.90	A/B/C/D	1-392	[»]
3QVS	X-ray	1.70	A	1-392	[»]
3QVT	X-ray	2.00	A	1-392	[»]
3QVW	X-ray	2.00	A	1-392	[»]
3QVX	X-ray	1.90	A	1-392	[»]
3QW2	X-ray	2.59	A/B/C/D	1-392	[»]

ProteinModelPortal

O28480.

SMR

O28480. Positions 1-392.

ModBase

Search...

Protein-protein interaction databases

STRING

224325.AF1794.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAB89456; AAB89456; AF_1794.

GeneID

1485017.

KEGG

afu:AF1794.

Phylogenomic databases

eggNOG

COG1260.

KO

K01858.

OMA

HAGNDGK.

ProtClustDB

CLSK782720.

Enzyme and pathway databases

BioCyc

AFUL224325:GJBC-1829-MONOMER.
MetaCyc:MONOMER-5064.

Family and domain databases

Gene3D

3.40.50.720. 2 hits.

InterPro

IPR002587. Myo-inos-1-P_Synthase.
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.

ProtoNet

Search...

Other

EvolutionaryTrace

O28480.

Entry information

Entry name

O28480_ARCFU

Accession

Primary (citable) accession number: O28480

Entry history

Integrated into UniProtKB/TrEMBL:	January 1, 1998
Last sequence update:	January 1, 1998
Last modified:	May 1, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)