KGUA_MYCTU
ID KGUA_MYCTU Reviewed; 208 AA.
AC P9WKE9; L0T9H5; P0A5I4; P71659;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Guanylate kinase;
DE EC=2.7.4.8;
DE AltName: Full=GMP kinase;
GN Name=gmk; OrderedLocusNames=Rv1389; ORFNames=MTCY21B4.06;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Essential for recycling GMP and indirectly, cGMP.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + GMP = ADP + GDP; Xref=Rhea:RHEA:20780,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58115, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:456216; EC=2.7.4.8;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the guanylate kinase family. {ECO:0000305}.
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DR EMBL; AL123456; CCP44148.1; -; Genomic_DNA.
DR PIR; C70899; C70899.
DR RefSeq; NP_215905.1; NC_000962.3.
DR RefSeq; WP_003900331.1; NZ_NVQJ01000050.1.
DR PDB; 1S4Q; X-ray; 2.16 A; A=2-208.
DR PDB; 1Z8F; X-ray; 2.50 A; A=2-208.
DR PDB; 1ZNW; X-ray; 2.10 A; A=2-208.
DR PDB; 1ZNX; X-ray; 2.35 A; A=2-208.
DR PDB; 1ZNY; X-ray; 2.30 A; A=2-208.
DR PDB; 1ZNZ; X-ray; 2.50 A; A=2-208.
DR PDBsum; 1S4Q; -.
DR PDBsum; 1Z8F; -.
DR PDBsum; 1ZNW; -.
DR PDBsum; 1ZNX; -.
DR PDBsum; 1ZNY; -.
DR PDBsum; 1ZNZ; -.
DR AlphaFoldDB; P9WKE9; -.
DR SMR; P9WKE9; -.
DR STRING; 83332.Rv1389; -.
DR DrugBank; DB01942; Formic acid.
DR iPTMnet; P9WKE9; -.
DR PaxDb; P9WKE9; -.
DR DNASU; 886787; -.
DR GeneID; 45425367; -.
DR GeneID; 886787; -.
DR KEGG; mtu:Rv1389; -.
DR TubercuList; Rv1389; -.
DR eggNOG; COG3709; Bacteria.
DR OMA; EWAVVHG; -.
DR PhylomeDB; P9WKE9; -.
DR BRENDA; 2.7.4.8; 3445.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004017; F:adenylate kinase activity; IDA:MTBBASE.
DR GO; GO:0005524; F:ATP binding; IDA:MTBBASE.
DR GO; GO:0019003; F:GDP binding; IDA:MTBBASE.
DR GO; GO:0019002; F:GMP binding; IDA:MTBBASE.
DR GO; GO:0004385; F:guanylate kinase activity; IDA:MTBBASE.
DR GO; GO:0000287; F:magnesium ion binding; IDA:MTBBASE.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00328; Guanylate_kinase; 1.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR017665; Guanylate_kinase.
DR InterPro; IPR020590; Guanylate_kinase_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00625; Guanylate_kin; 1.
DR SMART; SM00072; GuKc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR03263; guanyl_kin; 1.
DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cytoplasm; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:21969609"
FT CHAIN 2..208
FT /note="Guanylate kinase"
FT /id="PRO_0000170570"
FT DOMAIN 21..201
FT /note="Guanylate kinase-like"
FT BINDING 28..35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:21969609"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:1ZNW"
FT HELIX 34..44
FT /evidence="ECO:0007829|PDB:1ZNW"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:1ZNW"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:1ZNW"
FT HELIX 74..82
FT /evidence="ECO:0007829|PDB:1ZNW"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:1ZNW"
FT TURN 93..96
FT /evidence="ECO:0007829|PDB:1ZNW"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:1ZNW"
FT HELIX 103..111
FT /evidence="ECO:0007829|PDB:1ZNW"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:1ZNW"
FT HELIX 122..131
FT /evidence="ECO:0007829|PDB:1ZNW"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:1ZNW"
FT HELIX 145..153
FT /evidence="ECO:0007829|PDB:1ZNW"
FT HELIX 160..175
FT /evidence="ECO:0007829|PDB:1ZNW"
FT HELIX 176..179
FT /evidence="ECO:0007829|PDB:1ZNW"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:1ZNW"
FT HELIX 189..200
FT /evidence="ECO:0007829|PDB:1ZNW"
SQ SEQUENCE 208 AA; 22095 MW; 3D2948315974549F CRC64;
MSVGEGPDTK PTARGQPAAV GRVVVLSGPS AVGKSTVVRC LRERIPNLHF SVSATTRAPR
PGEVDGVDYH FIDPTRFQQL IDQGELLEWA EIHGGLHRSG TLAQPVRAAA ATGVPVLIEV
DLAGARAIKK TMPEAVTVFL APPSWQDLQA RLIGRGTETA DVIQRRLDTA RIELAAQGDF
DKVVVNRRLE SACAELVSLL VGTAPGSP
