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Database: UniProt
Entry: R7H3D0_9BACT
LinkDB: R7H3D0_9BACT
Original site: R7H3D0_9BACT 
ID   R7H3D0_9BACT            Unreviewed;       188 AA.
AC   R7H3D0;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 46.
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=BN741_01755 {ECO:0000313|EMBL:CDE33786.1};
OS   Leyella stercorea CAG:629.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Leyella.
OX   NCBI_TaxID=1263103 {ECO:0000313|EMBL:CDE33786.1, ECO:0000313|Proteomes:UP000018072};
RN   [1] {ECO:0000313|EMBL:CDE33786.1, ECO:0000313|Proteomes:UP000018072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:629 {ECO:0000313|Proteomes:UP000018072};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Essential for recycling GMP and indirectly, cGMP.
CC       {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; Evidence={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:CDE33786.1}.
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DR   EMBL; CBIT010000202; CDE33786.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7H3D0; -.
DR   STRING; 1263103.BN741_01755; -.
DR   Proteomes; UP000018072; 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; 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          2..183
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50052"
FT   BINDING         9..16
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00328"
SQ   SEQUENCE   188 AA;  21737 MW;  5C0C5CC06CB9E2CF CRC64;
     MGKLIIFSAP SGSGKSTIIN RLMQRPELHL AFSISCTSRA PRGTEQNGVE YFFITPEEFR
     ERIRRDEFLE YEEVYQDRFY GTLKEQVETQ AARGENVVFD LDVKGGCNIK KFYGDRALSL
     FIQPPSVEEL RRRLVGRATD APEVIEQRIA RAEFELSQAP KFDRIIINDD LEKAVEETYE
     AIRSFIEE
//
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