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Database: UniProt
Entry: U1LEA2_9MICO
LinkDB: U1LEA2_9MICO
Original site: U1LEA2_9MICO 
ID   U1LEA2_9MICO            Unreviewed;       306 AA.
AC   U1LEA2;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 44.
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=L332_14185 {ECO:0000313|EMBL:ERG65583.1};
OS   Agrococcus pavilionensis RW1.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Agrococcus.
OX   NCBI_TaxID=1330458 {ECO:0000313|EMBL:ERG65583.1, ECO:0000313|Proteomes:UP000016462};
RN   [1] {ECO:0000313|EMBL:ERG65583.1, ECO:0000313|Proteomes:UP000016462}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RW1 {ECO:0000313|EMBL:ERG65583.1,
RC   ECO:0000313|Proteomes:UP000016462};
RX   PubMed=23814108;
RA   White R.A.III., Grassa C.J., Suttle C.A.;
RT   "First draft genome sequence from a member of the genus agrococcus,
RT   isolated from modern microbialites.";
RL   Genome Announc. 1:e00391-13(2013).
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:ERG65583.1}.
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DR   EMBL; ASHR01000001; ERG65583.1; -; Genomic_DNA.
DR   AlphaFoldDB; U1LEA2; -.
DR   Proteomes; UP000016462; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000016462};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00328}.
FT   DOMAIN          119..298
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50052"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         126..133
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00328"
SQ   SEQUENCE   306 AA;  33530 MW;  C06E92561453D288 CRC64;
     MTGSRDRGVP ERSIPDPGAA GRAAIEARRA RAAVKRALAA GQRGPRDVAE RAWQEPDGVE
     ARLRVPEYFG SLRGMGPKRV ETLMRELAIA PSKRLGGLGG LQRERVRAWL DVVDPSRRPR
     LIVLAGPTAV GKGTVAQYVR EHFPQIRHSV SATTRAPRPG EIDGVHYAFV SDAEFDRMVD
     EGEFLEWATV HNLSRYGTPR SSVQAALDEG SSVLLEIDLQ GARQVRESFP DAVLLFLAPP
     SWDELVRRLV GRGTETPAER AKRLETAKVE LASQPEFDAT IVNSDVAEAA HEVVERILAA
     EAEARE
//
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