KGUA_ANAPZ
ID KGUA_ANAPZ Reviewed; 210 AA.
AC Q2GLF7;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Guanylate kinase {ECO:0000255|HAMAP-Rule:MF_00328};
DE EC=2.7.4.8 {ECO:0000255|HAMAP-Rule:MF_00328};
DE AltName: Full=GMP kinase {ECO:0000255|HAMAP-Rule:MF_00328};
GN Name=gmk {ECO:0000255|HAMAP-Rule:MF_00328}; OrderedLocusNames=APH_0170;
OS Anaplasma phagocytophilum (strain HZ).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Anaplasma; phagocytophilum group.
OX NCBI_TaxID=212042;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HZ;
RX PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M.,
RA Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W.C.,
RA Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P., Daugherty S.C.,
RA Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H., Selengut J.D.,
RA Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R.,
RA Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.;
RT "Comparative genomics of emerging human ehrlichiosis agents.";
RL PLoS Genet. 2:208-222(2006).
CC -!- FUNCTION: Essential for recycling GMP and indirectly, cGMP.
CC {ECO:0000255|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:0000255|HAMAP-
CC Rule:MF_00328};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00328}.
CC -!- SIMILARITY: Belongs to the guanylate kinase family. {ECO:0000255|HAMAP-
CC Rule:MF_00328}.
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DR EMBL; CP000235; ABD43557.1; -; Genomic_DNA.
DR RefSeq; WP_011450318.1; NC_007797.1.
DR PDB; 3LNC; X-ray; 1.95 A; A/B=1-210.
DR PDBsum; 3LNC; -.
DR AlphaFoldDB; Q2GLF7; -.
DR SMR; Q2GLF7; -.
DR STRING; 212042.APH_0170; -.
DR EnsemblBacteria; ABD43557; ABD43557; APH_0170.
DR GeneID; 56368342; -.
DR KEGG; aph:APH_0170; -.
DR eggNOG; COG0194; Bacteria.
DR HOGENOM; CLU_001715_1_2_5; -.
DR OMA; EWAVVHG; -.
DR EvolutionaryTrace; Q2GLF7; -.
DR Proteomes; UP000001943; 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 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; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..210
FT /note="Guanylate kinase"
FT /id="PRO_0000266285"
FT DOMAIN 6..186
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00328"
FT BINDING 13..20
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00328"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:3LNC"
FT HELIX 22..27
FT /evidence="ECO:0007829|PDB:3LNC"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:3LNC"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:3LNC"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:3LNC"
FT HELIX 60..68
FT /evidence="ECO:0007829|PDB:3LNC"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:3LNC"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:3LNC"
FT HELIX 90..96
FT /evidence="ECO:0007829|PDB:3LNC"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:3LNC"
FT HELIX 106..115
FT /evidence="ECO:0007829|PDB:3LNC"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:3LNC"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:3LNC"
FT HELIX 130..135
FT /evidence="ECO:0007829|PDB:3LNC"
FT HELIX 152..159
FT /evidence="ECO:0007829|PDB:3LNC"
FT HELIX 160..164
FT /evidence="ECO:0007829|PDB:3LNC"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:3LNC"
FT HELIX 174..189
FT /evidence="ECO:0007829|PDB:3LNC"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:3LNC"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:3LNC"
FT HELIX 198..205
FT /evidence="ECO:0007829|PDB:3LNC"
SQ SEQUENCE 210 AA; 23928 MW; A49B447B562D4E93 CRC64;
MLKSVGVILV LSSPSGCGKT TVANKLLEKQ KNNIVKSVSV TTRAARKGEK EGKDYYFVDR
EEFLRLCSNG EIIEHAEVFG NFYGVPRKNL EDNVDKGVST LLVIDWQGAF KFMEMMREHV
VSIFIMPPSM EELRRRLCGR RADDSEVVEA RLKGAAFEIS HCEAYDYVIV NEDIEETADR
ISNILRAEQM KTCRQVGLRE LLESRFPIED
