ID Q1PH30_ECOLX Unreviewed; 167 AA.
AC Q1PH30;
DT 16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=Adenylate kinase {ECO:0000256|RuleBase:RU003331};
DE EC=2.7.4.3 {ECO:0000256|RuleBase:RU003331};
DE Flags: Fragment;
GN Name=adk {ECO:0000313|EMBL:ABE28163.1};
GN ORFNames=UTI89_C0502 {ECO:0000313|EMBL:ABE28163.1};
OS Escherichia coli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562 {ECO:0000313|EMBL:ABE28163.1};
RN [1] {ECO:0000313|EMBL:ABE28163.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=E60-urine {ECO:0000313|EMBL:ABE28125.1}, E7-feces
RC {ECO:0000313|EMBL:ABE28160.1}, P1003-feces
RC {ECO:0000313|EMBL:ABE28328.1}, P1182-urine
RC {ECO:0000313|EMBL:ABE28136.1}, P1333-urine
RC {ECO:0000313|EMBL:ABE28135.1}, P31-urine
RC {ECO:0000313|EMBL:ABE28162.1}, P37-urine
RC {ECO:0000313|EMBL:ABE28129.1}, P41-urine
RC {ECO:0000313|EMBL:ABE28127.1}, T13-periurethra
RC {ECO:0000313|EMBL:ABE28118.1}, T15-urine
RC {ECO:0000313|EMBL:ABE28126.1}, T20-periurethra
RC {ECO:0000313|EMBL:ABE28116.1}, T21-urine
RC {ECO:0000313|EMBL:ABE28322.1}, T23-urine
RC {ECO:0000313|EMBL:ABE28133.1}, T26-periurethra
RC {ECO:0000313|EMBL:ABE28128.1}, T26-urine
RC {ECO:0000313|EMBL:ABE28131.1}, T27-urine
RC {ECO:0000313|EMBL:ABE28117.1}, T30-urine
RC {ECO:0000313|EMBL:ABE28134.1}, T31-periurethra
RC {ECO:0000313|EMBL:ABE28163.1}, T31-urine
RC {ECO:0000313|EMBL:ABE28157.1}, T35-periurethra
RC {ECO:0000313|EMBL:ABE28121.1}, T35-urine1
RC {ECO:0000313|EMBL:ABE28119.1}, T35-urine2
RC {ECO:0000313|EMBL:ABE28115.1}, T35-urine3
RC {ECO:0000313|EMBL:ABE28132.1}, T36-urine
RC {ECO:0000313|EMBL:ABE28120.1}, T41-periurethra
RC {ECO:0000313|EMBL:ABE28140.1}, T41-urine1
RC {ECO:0000313|EMBL:ABE28138.1}, T41-urine2
RC {ECO:0000313|EMBL:ABE28139.1}, T42-urine
RC {ECO:0000313|EMBL:ABE28159.1}, T51-urine
RC {ECO:0000313|EMBL:ABE28156.1}, T53-urine
RC {ECO:0000313|EMBL:ABE28122.1}, T57-urine
RC {ECO:0000313|EMBL:ABE28124.1}, T59-urine1
RC {ECO:0000313|EMBL:ABE28114.1}, T59-urine2
RC {ECO:0000313|EMBL:ABE28137.1}, T75-urine
RC {ECO:0000313|EMBL:ABE28123.1}, and T78-urine
RC {ECO:0000313|EMBL:ABE28130.1};
RX PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA Chen S.L., Hung C.S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA Gordon J.I.;
RT "Identification of genes subject to positive selection in uropathogenic
RT strains of Escherichia coli: a comparative genomics approach.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3;
CC Evidence={ECO:0000256|ARBA:ARBA00000582,
CC ECO:0000256|RuleBase:RU003331};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245,
CC ECO:0000256|RuleBase:RU003331}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|RuleBase:RU003331}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family.
CC {ECO:0000256|ARBA:ARBA00007220, ECO:0000256|RuleBase:RU003330}.
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DR EMBL; DQ441069; ABE28114.1; -; Genomic_DNA.
DR EMBL; DQ441070; ABE28115.1; -; Genomic_DNA.
DR EMBL; DQ441071; ABE28116.1; -; Genomic_DNA.
DR EMBL; DQ441072; ABE28117.1; -; Genomic_DNA.
DR EMBL; DQ441073; ABE28118.1; -; Genomic_DNA.
DR EMBL; DQ441074; ABE28119.1; -; Genomic_DNA.
DR EMBL; DQ441075; ABE28120.1; -; Genomic_DNA.
DR EMBL; DQ441076; ABE28121.1; -; Genomic_DNA.
DR EMBL; DQ441077; ABE28122.1; -; Genomic_DNA.
DR EMBL; DQ441078; ABE28123.1; -; Genomic_DNA.
DR EMBL; DQ441079; ABE28124.1; -; Genomic_DNA.
DR EMBL; DQ441080; ABE28125.1; -; Genomic_DNA.
DR EMBL; DQ441081; ABE28126.1; -; Genomic_DNA.
DR EMBL; DQ441082; ABE28127.1; -; Genomic_DNA.
DR EMBL; DQ441083; ABE28128.1; -; Genomic_DNA.
DR EMBL; DQ441084; ABE28129.1; -; Genomic_DNA.
DR EMBL; DQ441085; ABE28130.1; -; Genomic_DNA.
DR EMBL; DQ441086; ABE28131.1; -; Genomic_DNA.
DR EMBL; DQ441087; ABE28132.1; -; Genomic_DNA.
DR EMBL; DQ441088; ABE28133.1; -; Genomic_DNA.
DR EMBL; DQ441089; ABE28134.1; -; Genomic_DNA.
DR EMBL; DQ441090; ABE28135.1; -; Genomic_DNA.
DR EMBL; DQ441091; ABE28136.1; -; Genomic_DNA.
DR EMBL; DQ441092; ABE28137.1; -; Genomic_DNA.
DR EMBL; DQ441093; ABE28138.1; -; Genomic_DNA.
DR EMBL; DQ441094; ABE28139.1; -; Genomic_DNA.
DR EMBL; DQ441095; ABE28140.1; -; Genomic_DNA.
DR EMBL; DQ441111; ABE28156.1; -; Genomic_DNA.
DR EMBL; DQ441112; ABE28157.1; -; Genomic_DNA.
DR EMBL; DQ441114; ABE28159.1; -; Genomic_DNA.
DR EMBL; DQ441115; ABE28160.1; -; Genomic_DNA.
DR EMBL; DQ441117; ABE28162.1; -; Genomic_DNA.
DR EMBL; DQ441118; ABE28163.1; -; Genomic_DNA.
DR EMBL; DQ389026; ABE28322.1; -; Genomic_DNA.
DR EMBL; DQ389032; ABE28328.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1PH30; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004017; F:adenylate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01428; ADK; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00235; Adenylate_kinase_Adk; 1.
DR InterPro; IPR006259; Adenyl_kin_sub.
DR InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR InterPro; IPR033690; Adenylat_kinase_CS.
DR InterPro; IPR007862; Adenylate_kinase_lid-dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR01351; adk; 1.
DR PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1.
DR PANTHER; PTHR23359:SF206; UMP-CMP KINASE; 1.
DR Pfam; PF00406; ADK; 1.
DR Pfam; PF05191; ADK_lid; 1.
DR PRINTS; PR00094; ADENYLTKNASE.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003331};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU003330};
KW Nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022727};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003331};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003330}.
FT DOMAIN 106..141
FT /note="Adenylate kinase active site lid"
FT /evidence="ECO:0000259|Pfam:PF05191"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABE28163.1"
FT NON_TER 167
FT /evidence="ECO:0000313|EMBL:ABE28163.1"
SQ SEQUENCE 167 AA; 18794 MW; 633C121D221B4420 CRC64;
QFIMEKYGIP QISTGDMLRA AVKSGSELGK QAKDIMDAGK LVTDELVIAL VKERIAQEDC
RNGFLLDGFP RTIPQADAMK EAGINVDYVL EFDVPDELIV DRIVGRRVHA PSGRVYHVKF
NPPKVEGKDD VTGEELTTRK DDQEETVRKR LVEYHQMTAP LIGYYSK
//
