(data stored in ACNUC7421 zone)

SWISSPROT: D4YYQ0_SPHJU

ID   D4YYQ0_SPHJU            Unreviewed;       221 AA.
AC   D4YYQ0;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   07-JUN-2017, entry version 52.
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   ECO:0000313|EMBL:BAI95482.1};
GN   OrderedLocusNames=SJA_C1-06480 {ECO:0000313|EMBL:BAI95482.1};
OS   Sphingobium japonicum (strain NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI95482.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI95482.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101211 / UT26S {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(2010).
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. 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}.
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; AP010803; BAI95482.1; -; Genomic_DNA.
DR   ProteinModelPortal; D4YYQ0; -.
DR   STRING; 452662.SJA_C1-06480; -.
DR   EnsemblBacteria; BAI95482; BAI95482; SJA_C1-06480.
DR   KEGG; sjp:SJA_C1-06480; -.
DR   eggNOG; ENOG4105CC8; Bacteria.
DR   eggNOG; COG0563; LUCA.
DR   HOGENOM; HOG000238772; -.
DR   KO; K00939; -.
DR   OMA; EKFTSQG; -.
DR   OrthoDB; POG091H01SU; -.
DR   UniPathway; UPA00588; UER00649.
DR   Proteomes; UP000007753; Chromosome 1.
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:0008270; F:zinc ion 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; 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; 2.
DR   SUPFAM; SSF57774; SSF57774; 1.
DR   TIGRFAMs; TIGR01351; adk; 1.
DR   PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; D4YYQ0.
DR   SWISS-2DPAGE; D4YYQ0.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00235,
KW   ECO:0000256|RuleBase:RU003331, ECO:0000256|SAAS:SAAS00763703};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00235};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00235,
KW   ECO:0000256|RuleBase:RU003330, ECO:0000313|EMBL:BAI95482.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00235};
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:UP000007753};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00235,
KW   ECO:0000256|RuleBase:RU003330, ECO:0000313|EMBL:BAI95482.1};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00235}.
FT   DOMAIN      130    166       ADK_lid. {ECO:0000259|Pfam:PF05191}.
FT   NP_BIND      13     18       ATP. {ECO:0000256|HAMAP-Rule:MF_00235}.
FT   NP_BIND      88     91       AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.
FT   REGION       33     62       NMPbind. {ECO:0000256|HAMAP-Rule:
FT                                MF_00235}.
FT   METAL       133    133       Zinc; structural. {ECO:0000256|HAMAP-
FT                                Rule:MF_00235}.
FT   METAL       136    136       Zinc; structural. {ECO:0000256|HAMAP-
FT                                Rule:MF_00235}.
FT   METAL       153    153       Zinc; structural. {ECO:0000256|HAMAP-
FT                                Rule:MF_00235}.
FT   METAL       156    156       Zinc; structural. {ECO:0000256|HAMAP-
FT                                Rule:MF_00235}.
FT   BINDING      34     34       AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.
FT   BINDING      39     39       AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.
FT   BINDING      95     95       AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.
FT   BINDING     130    130       ATP. {ECO:0000256|HAMAP-Rule:MF_00235}.
FT   BINDING     164    164       AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.
FT   BINDING     175    175       AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.
FT   BINDING     203    203       ATP; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00235}.
SQ   SEQUENCE   221 AA;  23683 MW;  60E9C5232371A35C CRC64;
     MRDMNIILLG PPGAGKGTQA TRLVDSRAMV QLSTGDMLRA AVKAGTPIGL KAKAVMEAGE
     LVSDEIVSGI IGEALDALAP ETGVIFDGYP RTEAQAHSLD GILADRNRTL DHVIELEVDE
     DALVERITGR FTCATCGEGY HDRFKTPKVE GACDKCGGHE FKRRPDDNEE TVRTRMAEYR
     AKTAPILPIY EARGIVSRVD GMADMDDVTV AIAAILDGKA A
//

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