(data stored in ACNUC7421 zone)

SWISSPROT: C3MI55_SINFN

ID   C3MI55_SINFN            Unreviewed;       194 AA.
AC   C3MI55;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 65.
DE   RecName: Full=Adenylate kinase {ECO:0000256|HAMAP-Rule:MF_00235, ECO:0000256|RuleBase:RU003331, ECO:0000256|SAAS:SAAS00763757};
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=NGR_c06100 {ECO:0000313|EMBL:ACP24403.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP24403.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP24403.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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: ATP + AMP = 2 ADP. {ECO:0000256|HAMAP-
CC       Rule:MF_00235, ECO:0000256|RuleBase:RU003331,
CC       ECO:0000256|SAAS:SAAS00763738}.
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway;
CC       AMP from ADP: step 1/1. {ECO:0000256|HAMAP-Rule:MF_00235}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00235,
CC       ECO:0000256|RuleBase:RU003331}.
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. {ECO:0000256|HAMAP-
CC       Rule:MF_00235}.
CC   -!- SIMILARITY: Belongs to the adenylate kinase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00235, ECO:0000256|RuleBase:RU003330}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00235}.
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DR   EMBL; CP001389; ACP24403.1; -; Genomic_DNA.
DR   RefSeq; WP_012707188.1; NC_012587.1.
DR   RefSeq; YP_002825156.1; NC_012587.1.
DR   ProteinModelPortal; C3MI55; -.
DR   STRING; 394.NGR_c06100; -.
DR   EnsemblBacteria; ACP24403; ACP24403; NGR_c06100.
DR   GeneID; 7791836; -.
DR   KEGG; rhi:NGR_c06100; -.
DR   PATRIC; fig|394.7.peg.3425; -.
DR   eggNOG; ENOG4105CC8; Bacteria.
DR   eggNOG; COG0563; LUCA.
DR   HOGENOM; HOG000238772; -.
DR   KO; K00939; -.
DR   OrthoDB; POG091H01SU; -.
DR   UniPathway; UPA00588; UER00649.
DR   Proteomes; UP000001054; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004017; F:adenylate kinase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
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; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR23359; PTHR23359; 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; C3MI55.
DR   SWISS-2DPAGE; C3MI55.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00235,
KW   ECO:0000256|RuleBase:RU003331, ECO:0000256|SAAS:SAAS00763703};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00235};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00235,
KW   ECO:0000256|RuleBase:RU003330, ECO:0000313|EMBL:ACP24403.1};
KW   Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00235};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00235,
KW   ECO:0000256|RuleBase:RU003331};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00235,
KW   ECO:0000256|RuleBase:RU003330}.
FT   NP_BIND      11     16       ATP. {ECO:0000256|HAMAP-Rule:MF_00235}.
FT   NP_BIND      86     89       AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.
FT   REGION       31     60       NMPbind. {ECO:0000256|HAMAP-Rule:
FT                                MF_00235}.
FT   BINDING      32     32       AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.
FT   BINDING      37     37       AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.
FT   BINDING      93     93       AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.
FT   BINDING     128    128       ATP. {ECO:0000256|HAMAP-Rule:MF_00235}.
FT   BINDING     140    140       AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.
FT   BINDING     151    151       AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.
FT   BINDING     179    179       ATP; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00235}.
SQ   SEQUENCE   194 AA;  21486 MW;  BB137BDE4A88DEC5 CRC64;
     MVNLVLLGPP GAGKGTQAER LVRDYDLLHI STGDLLRDAI KAQSPLGRKA KMAVDEGKLV
     PDEVVVGLVE ERLTDKEPGQ GFILDGFPRT IAQAGALERL LESMQVPLDH VILFDIPIRL
     LEERIAKRAE QTRSAGAQPR TDDSPEVLKK RIEEFARATA ALSPFYEQNG LLRRVDASED
     IERVATQIRD FLQP
//

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