(data stored in ACNUC7421 zone)

SWISSPROT: A0A0F6BHT6_GEOS0

ID   A0A0F6BHT6_GEOS0        Unreviewed;       216 AA.
AC   A0A0F6BHT6;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   08-MAY-2019, entry version 26.
DE   RecName: Full=Adenylate kinase {ECO:0000256|HAMAP-Rule:MF_00235, ECO:0000256|RuleBase:RU003331, ECO:0000256|SAAS:SAAS00914410};
DE            Short=AK {ECO:0000256|HAMAP-Rule:MF_00235};
DE            EC=2.7.4.3 {ECO:0000256|HAMAP-Rule:MF_00235, ECO:0000256|RuleBase:RU003331, ECO:0000256|SAAS:SAAS00763757};
DE   AltName: Full=ATP-AMP transphosphorylase {ECO:0000256|HAMAP-Rule:MF_00235};
DE   AltName: Full=ATP:AMP phosphotransferase {ECO:0000256|HAMAP-Rule:MF_00235};
DE   AltName: Full=Adenylate monophosphate kinase {ECO:0000256|HAMAP-Rule:MF_00235};
GN   Name=adk {ECO:0000256|HAMAP-Rule:MF_00235};
GN   OrderedLocusNames=GY4MC1_0131 {ECO:0000313|EMBL:ADP72987.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP72987.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP72987.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP72987.1,
RC   ECO:0000313|Proteomes:UP000002034};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible transfer of the terminal
CC       phosphate group between ATP and AMP. Plays an important role in
CC       cellular energy homeostasis and in adenine nucleotide metabolism.
CC       {ECO:0000256|HAMAP-Rule:MF_00235}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216;
CC         EC=2.7.4.3; Evidence={ECO:0000256|HAMAP-Rule:MF_00235,
CC         ECO:0000256|RuleBase:RU003331, ECO:0000256|SAAS:SAAS01123758};
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway;
CC       AMP from ADP: step 1/1. {ECO:0000256|HAMAP-Rule:MF_00235,
CC       ECO:0000256|SAAS:SAAS00914379}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00235,
CC       ECO:0000256|RuleBase:RU003331, ECO:0000256|SAAS:SAAS00914390}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00235,
CC       ECO:0000256|RuleBase:RU003331}.
CC   -!- DOMAIN: Consists of three domains, a large central CORE domain and
CC       two small peripheral domains, NMPbind and LID, which undergo
CC       movements during catalysis. The LID domain closes over the site of
CC       phosphoryl transfer upon ATP binding. Assembling and dissambling
CC       the active center during each catalytic cycle provides an
CC       effective means to prevent ATP hydrolysis. Some bacteria have
CC       evolved a zinc-coordinating structure that stabilizes the LID
CC       domain. {ECO:0000256|HAMAP-Rule:MF_00235}.
CC   -!- SIMILARITY: Belongs to the adenylate kinase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00235, ECO:0000256|RuleBase:RU003330}.
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DR   EMBL; CP002293; ADP72987.1; -; Genomic_DNA.
DR   RefSeq; WP_003247615.1; NC_014650.1.
DR   EnsemblBacteria; ADP72987; ADP72987; GY4MC1_0131.
DR   KEGG; gmc:GY4MC1_0131; -.
DR   KO; K00939; -.
DR   OMA; EKFTSQG; -.
DR   OrthoDB; 1491686at2; -.
DR   BioCyc; GSP581103:G1GOQ-158-MONOMER; -.
DR   UniPathway; UPA00588; UER00649.
DR   Proteomes; UP000002034; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004017; F:adenylate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway.
DR   CDD; cd01428; ADK; 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   PANTHER; PTHR23359; PTHR23359; 1.
DR   Pfam; PF05191; ADK_lid; 1.
DR   PRINTS; PR00094; ADENYLTKNASE.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01351; adk; 1.
DR   PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0F6BHT6.
DR   SWISS-2DPAGE; A0A0F6BHT6.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00235,
KW   ECO:0000256|RuleBase:RU003331, ECO:0000256|SAAS:SAAS00763703};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002034};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00235};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00235,
KW   ECO:0000256|RuleBase:RU003330, ECO:0000313|EMBL:ADP72987.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00235};
KW   Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00235,
KW   ECO:0000256|SAAS:SAAS00914406};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00235,
KW   ECO:0000256|RuleBase:RU003331};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00235,
KW   ECO:0000256|RuleBase:RU003330};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00235}.
FT   DOMAIN      127    162       ADK_lid. {ECO:0000259|Pfam:PF05191}.
FT   NP_BIND      10     15       ATP. {ECO:0000256|HAMAP-Rule:MF_00235}.
FT   NP_BIND      57     59       AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.
FT   NP_BIND      85     88       AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.
FT   NP_BIND     136    137       ATP. {ECO:0000256|HAMAP-Rule:MF_00235}.
FT   REGION       30     59       NMPbind. {ECO:0000256|HAMAP-Rule:
FT                                MF_00235}.
FT   REGION      126    163       LID. {ECO:0000256|HAMAP-Rule:MF_00235}.
FT   METAL       130    130       Zinc; structural. {ECO:0000256|HAMAP-
FT                                Rule:MF_00235}.
FT   METAL       133    133       Zinc; structural. {ECO:0000256|HAMAP-
FT                                Rule:MF_00235}.
FT   METAL       150    150       Zinc; structural. {ECO:0000256|HAMAP-
FT                                Rule:MF_00235}.
FT   METAL       153    153       Zinc; structural. {ECO:0000256|HAMAP-
FT                                Rule:MF_00235}.
FT   BINDING      31     31       AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.
FT   BINDING      36     36       AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.
FT   BINDING      92     92       AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.
FT   BINDING     127    127       ATP. {ECO:0000256|HAMAP-Rule:MF_00235}.
FT   BINDING     160    160       AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.
FT   BINDING     171    171       AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.
FT   BINDING     199    199       ATP; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00235}.
SQ   SEQUENCE   216 AA;  24116 MW;  CEE9D2395E4A2F33 CRC64;
     MNLVLMGLPG AGKGTQAEKI VETYGIPHIS TGDMFRAAIK EGTPLGLQAK EYMDRGDLVP
     DEVTIGIVRE RLSKDDCHKG FLLDGFPRTV AQAEALENIL AELTRSIDYV IHIQVDKDIL
     MERLTGRRIC KNCGATYHLV FNPPANPGVC DKCGGELYQR ADDNEETVAN RLEVNVKQMQ
     PLLEFYEKKG YLRHIDGQQD IEKVFADIRE LLGGLQ
//

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