Guanylate kinase - Mycobacterium tuberculosis

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P0A5I4 (KGUA_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 48. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Guanylate kinase
EC=2.7.4.8

Alternative name(s):
GMP kinase

Gene names

Name:	gmk
Ordered Locus Names:	Rv1389, MT1434
ORF Names:	MTCY21B4.06

Organism

Mycobacterium tuberculosis

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	208 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Essential for recycling GMP and indirectly, cGMP By similarity. HAMAP MF_00328
Catalytic activity	ATP + GMP = ADP + GDP. HAMAP MF_00328
Subcellular location	Cytoplasm By similarity HAMAP MF_00328.
Sequence similarities	Belongs to the guanylate kinase family. Contains 1 guanylate kinase-like domain.
Sequence caution	The sequence AAK45699.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	growth Inferred from mutant phenotype. Source: MTBBASE purine nucleotide metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from direct assay. Source: MTBBASE GDP binding Inferred from direct assay. Source: MTBBASE GMP binding Inferred from direct assay. Source: MTBBASE adenylate kinase activity Inferred from direct assay. Source: MTBBASE guanylate kinase activity Inferred from direct assay. Source: MTBBASE magnesium ion binding Inferred from direct assay. Source: MTBBASE
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 208

208

Guanylate kinase HAMAP MF_00328

PRO_0000170570

Regions

Domain

21 – 201

181

Guanylate kinase-like

Nucleotide binding

28 – 35

ATP By similarity

Secondary structure

208

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A5I4 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 3D2948315974549F
Show »

FASTA

208

22,095

        10         20         30         40         50         60 
MSVGEGPDTK PTARGQPAAV GRVVVLSGPS AVGKSTVVRC LRERIPNLHF SVSATTRAPR 

        70         80         90        100        110        120 
PGEVDGVDYH FIDPTRFQQL IDQGELLEWA EIHGGLHRSG TLAQPVRAAA ATGVPVLIEV 

       130        140        150        160        170        180 
DLAGARAIKK TMPEAVTVFL APPSWQDLQA RLIGRGTETA DVIQRRLDTA RIELAAQGDF 

       190        200 
DKVVVNRRLE SACAELVSLL VGTAPGSP

« Hide

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. Barrell B.G. Nature 393:537-544(1998) [PubMed: 9634230] [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. Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BX842576 Genomic DNA. Translation: CAB02172.1.
AE000516 Genomic DNA. Translation: AAK45699.1. Different initiation.

PIR

C70899.

RefSeq

NP_215905.1. NC_000962.2.
NP_335885.1. NC_002755.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1S4Q	X-ray	2.16	A	2-208	[»]
1Z8F	X-ray	2.50	A	2-208	[»]
1ZNW	X-ray	2.10	A	2-208	[»]
1ZNX	X-ray	2.35	A	2-208	[»]
1ZNY	X-ray	2.30	A	2-208	[»]
1ZNZ	X-ray	2.50	A	2-208	[»]

ProteinModelPortal

P0A5I4.

SMR

P0A5I4. Positions 20-202.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBMYCT00000001910; EBMYCP00000001910; EBMYCG00000001908.
EBMYCT00000070109; EBMYCP00000068168; EBMYCG00000070104.

GeneID

886787.
924551.

GenomeReviews

Gene locus MT1434 in contig AE000516_GR.
Gene locus Rv1389 in contig AL123456_GR.

KEGG

mtc:MT1434.
mtu:Rv1389.

PATRIC

18124922. VBIMycTub22151_1575.

TIGR

MT1434.

Organism-specific databases

TubercuList

Rv1389.

Phylogenomic databases

GeneTree

EBGT00050000017746.

HOGENOM

HBG671982.

OMA

EWAEFAG.

PhylomeDB

P0A5I4.

ProtClustDB

PRK00300.

Family and domain databases

HAMAP

MF_00328. Guanylate_kinase.
[Tree]

InterPro

IPR008144. Guanylate_kin.
IPR008145. Guanylate_kin/L-typ_Ca_channel.
IPR020590. Guanylate_kinase_CS.
IPR017665. Guanylate_kinase_sub.
[Graphical view]

K00942.

Pfam

PF00625. Guanylate_kin. 1 hit.
[Graphical view]

SMART

SM00072. GuKc. 1 hit.
[Graphical view]

TIGRFAMs

TIGR03263. Guanyl_kin. 1 hit.

PROSITE

PS00856. GUANYLATE_KINASE_1. 1 hit.
PS50052. GUANYLATE_KINASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

KGUA_MYCTU

Accession

Primary (citable) accession number: P0A5I4
Secondary accession number(s): P71659

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	March 15, 2005
Last modified:	January 25, 2012
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents