ID A0A1S2MWW0_9MICO Unreviewed; 303 AA.
AC A0A1S2MWW0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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 ORFNames=BK819_07925 {ECO:0000313|EMBL:OIJ33688.1};
OS Microbacterium sp. LCT-H2.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1914306 {ECO:0000313|EMBL:OIJ33688.1, ECO:0000313|Proteomes:UP000179624};
RN [1] {ECO:0000313|EMBL:OIJ33688.1, ECO:0000313|Proteomes:UP000179624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LCT-H2 {ECO:0000313|EMBL:OIJ33688.1,
RC ECO:0000313|Proteomes:UP000179624};
RA Huang B.;
RT "Draft genome sequence of strain LCT isolated from the Shenzhou X
RT spacecraft of China.";
RL Submitted (OCT-2016) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OIJ33688.1}.
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DR EMBL; MODW01000002; OIJ33688.1; -; Genomic_DNA.
DR RefSeq; WP_071328628.1; NZ_MODW01000002.1.
DR AlphaFoldDB; A0A1S2MWW0; -.
DR OrthoDB; 9808150at2; -.
DR Proteomes; UP000179624; Unassembled WGS sequence.
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; 1.10.8.50; -; 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; IPR047806; IHF_actinobact.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; NF041260; actino_IHF; 1.
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 120..299
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT BINDING 127..134
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00328"
SQ SEQUENCE 303 AA; 33622 MW; 17CC42E74F6AC186 CRC64;
MAEERRTVPE VDRAAAARRA VERRRARASV KRDLTMRVVT PQSVLHRATE DPDSVEGSMR
ITDFLLALPA IGAGKRDRVL EQLHISPVKR LGGLGARQRR VLEEWLDERF PVSTPRGARS
RLLVLAGPTA VGKGTVAAHI RENNPEIHLS VSATTRPPRP GEIDGVHYYF VDDAEFDRLI
ADGELLEYAV VHNRSRYGTP RAPIDAALAE GKTVLLEIDL QGARQVREAE PSATLIFLLP
PSWDELVHRL VGRGTEDAEE RSRRLRTAKV ELAAQNEFDH LIVNEDVATA AREVVDLSTS
SAR
//
