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Database: UniProt
Entry: A0A1X2C0Z2_9MYCO
LinkDB: A0A1X2C0Z2_9MYCO
Original site: A0A1X2C0Z2_9MYCO 
ID   A0A1X2C0Z2_9MYCO        Unreviewed;       208 AA.
AC   A0A1X2C0Z2;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Guanylate kinase {ECO:0000256|ARBA:ARBA00016296, ECO:0000256|HAMAP-Rule:MF_00328};
DE            EC=2.7.4.8 {ECO:0000256|ARBA:ARBA00012961, ECO:0000256|HAMAP-Rule:MF_00328};
DE   AltName: Full=GMP kinase {ECO:0000256|ARBA:ARBA00030128, ECO:0000256|HAMAP-Rule:MF_00328};
GN   Name=gmk {ECO:0000256|HAMAP-Rule:MF_00328,
GN   ECO:0000313|EMBL:BBX60991.1};
GN   ORFNames=AWC23_01305 {ECO:0000313|EMBL:ORW69558.1}, MSAS_01650
GN   {ECO:0000313|EMBL:BBX60991.1};
OS   Mycobacterium saskatchewanense.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium simiae complex.
OX   NCBI_TaxID=220927 {ECO:0000313|EMBL:BBX60991.1, ECO:0000313|Proteomes:UP000467517};
RN   [1] {ECO:0000313|EMBL:ORW69558.1, ECO:0000313|Proteomes:UP000193387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44616 {ECO:0000313|EMBL:ORW69558.1,
RC   ECO:0000313|Proteomes:UP000193387};
RA   Tarcisio F., Conor M., Antonella G., Elisabetta G., Giulia F.S., Sara T.,
RA   Anna F., Clotilde B., Roberto B., Veronica D.S., Fabio R., Monica P.,
RA   Olivier J., Enrico T., Nicola S.;
RT   "The new phylogeny of the genus Mycobacterium.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BBX60991.1, ECO:0000313|Proteomes:UP000467517}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 13016 {ECO:0000313|EMBL:BBX60991.1,
RC   ECO:0000313|Proteomes:UP000467517};
RX   PubMed=31287781;
RA   Matsumoto Y., Kinjo T., Motooka D., Nabeya D., Jung N., Uechi K., Horii T.,
RA   Iida T., Fujita J., Nakamura S.;
RT   "Comprehensive subspecies identification of 175 nontuberculous mycobacteria
RT   species based on 7547 genomic profiles.";
RL   Emerg. Microbes Infect. 8:1043-1053(2019).
RN   [3] {ECO:0000313|EMBL:BBX60991.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JCM 13016 {ECO:0000313|EMBL:BBX60991.1};
RA   Matsumoto Y., Motooka D., Nakamura S.;
RL   Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Essential for recycling GMP and indirectly, cGMP.
CC       {ECO:0000256|ARBA:ARBA00003531, ECO:0000256|HAMAP-Rule:MF_00328}.
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         Evidence={ECO:0000256|ARBA:ARBA00000283, ECO:0000256|HAMAP-
CC         Rule:MF_00328};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00328}.
CC   -!- SIMILARITY: Belongs to the guanylate kinase family.
CC       {ECO:0000256|ARBA:ARBA00005790, ECO:0000256|HAMAP-Rule:MF_00328}.
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DR   EMBL; AP022573; BBX60991.1; -; Genomic_DNA.
DR   EMBL; LQPR01000045; ORW69558.1; -; Genomic_DNA.
DR   STRING; 220927.AWC23_01305; -.
DR   KEGG; msak:MSAS_01650; -.
DR   OrthoDB; 9808150at2; -.
DR   Proteomes; UP000193387; Unassembled WGS sequence.
DR   Proteomes; UP000467517; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004385; F:guanylate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00071; GMPK; 1.
DR   Gene3D; 3.30.63.10; Guanylate Kinase phosphate binding domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR03263; guanyl_kin; 1.
DR   PANTHER; PTHR23117:SF13; GUANYLATE KINASE; 1.
DR   PANTHER; PTHR23117; GUANYLATE KINASE-RELATED; 1.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   SMART; SM00072; GuKc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00328}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00328};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00328};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00328};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00328}.
FT   DOMAIN          21..201
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50052"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         28..35
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00328"
SQ   SEQUENCE   208 AA;  22084 MW;  9D351C5C9DAC2B61 CRC64;
     MSAGGGPDTE RGTRPEPKGK GRVVVLSGPS AVGKSTVVRC LRERIPDLHF SVSATTRAPR
     PGEVDGVDYH FVTPARFQQL IDEGALLEWA EIHGGLHRSG TLAEPVRAAT AAGRPVLIEV
     DLAGARAVKK AMPEAITVFL APPSWEDLQA RLLGRGTETP EAIQRRLETA RVEMAAQGDF
     DEVVVNRRLE SACAELVSLL VGTAPGPA
//
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