(data stored in ACNUC8465 zone)

SWISSPROT: B6H1V9_PENRW

ID   B6H1V9_PENRW            Unreviewed;       254 AA.
AC   B6H1V9;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   07-JUN-2017, entry version 63.
DE   RecName: Full=GTP:AMP phosphotransferase, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03169};
DE            EC=2.7.4.10 {ECO:0000256|HAMAP-Rule:MF_03169};
DE   AltName: Full=Adenylate kinase 3 {ECO:0000256|HAMAP-Rule:MF_03169};
DE            Short=AK 3 {ECO:0000256|HAMAP-Rule:MF_03169};
GN   Name=ADK2 {ECO:0000256|HAMAP-Rule:MF_03169};
GN   ORFNames=Pc13g03220 {ECO:0000313|EMBL:CAP91391.1}, PCH_Pc13g03220
GN   {ECO:0000313|EMBL:CAP91391.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 /
OS   Wisconsin 54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP91391.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP91391.1, ECO:0000313|Proteomes:UP000000724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC   {ECO:0000313|Proteomes:UP000000724};
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A.,
RA   van der Klei I.J., van Peij N.N.M.E., Veenhuis M., von Doehren H.,
RA   Wagner C., Wortman J.R., Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
CC   -!- FUNCTION: Involved in maintaining the homeostasis of cellular
CC       nucleotides by catalyzing the interconversion of nucleoside
CC       phosphates. Has GTP:AMP phosphotransferase and ITP:AMP
CC       phosphotransferase activities. {ECO:0000256|HAMAP-Rule:MF_03169}.
CC   -!- CATALYTIC ACTIVITY: NTP + AMP = NDP + ADP. {ECO:0000256|HAMAP-
CC       Rule:MF_03169}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_03169}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000256|HAMAP-
CC       Rule:MF_03169}.
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 GTP binding. Assembling and dissambling
CC       the active center during each catalytic cycle provides an
CC       effective means to prevent GTP hydrolysis. {ECO:0000256|HAMAP-
CC       Rule:MF_03169}.
CC   -!- SIMILARITY: Belongs to the adenylate kinase family. AK3 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_03169}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_03169}.
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DR   EMBL; AM920428; CAP91391.1; -; Genomic_DNA.
DR   RefSeq; XP_002558760.1; XM_002558714.1.
DR   ProteinModelPortal; B6H1V9; -.
DR   STRING; 500485.XP_002558760.1; -.
DR   EnsemblFungi; CAP91391; CAP91391; PCH_Pc13g03220.
DR   GeneID; 8313422; -.
DR   KEGG; pcs:Pc13g03220; -.
DR   eggNOG; KOG3078; Eukaryota.
DR   eggNOG; COG0563; LUCA.
DR   HOGENOM; HOG000238772; -.
DR   KO; K00939; -.
DR   OMA; RVKNRWI; -.
DR   OrthoDB; EOG092C5OQU; -.
DR   BioCyc; PCHR:PC13G03220-MONOMER; -.
DR   Proteomes; UP000000724; Contig Pc00c13.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0004017; F:adenylate kinase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046899; F:nucleoside triphosphate adenylate kinase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006172; P:ADP biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0046033; P:AMP metabolic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0046039; P:GTP metabolic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0046041; P:ITP metabolic process; IEA:UniProtKB-HAMAP.
DR   CDD; cd01428; ADK; 1.
DR   HAMAP; MF_00235; Adenylate_kinase_Adk; 1.
DR   HAMAP; MF_03169; Adenylate_kinase_AK3; 1.
DR   InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR   InterPro; IPR033690; Adenylat_kinase_CS.
DR   InterPro; IPR007862; Adenylate_kinase_lid-dom.
DR   InterPro; IPR028586; AK3/Ak4_mitochondrial.
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   PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; B6H1V9.
DR   SWISS-2DPAGE; B6H1V9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000724};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_03169};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_03169,
KW   ECO:0000256|RuleBase:RU003330};
KW   Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03169};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03169};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000724};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03169,
KW   ECO:0000256|RuleBase:RU003330}.
FT   DOMAIN      165    200       ADK_lid. {ECO:0000259|Pfam:PF05191}.
FT   NP_BIND      21     26       GTP. {ECO:0000256|HAMAP-Rule:MF_03169}.
FT   NP_BIND     128    131       AMP. {ECO:0000256|HAMAP-Rule:MF_03169}.
FT   NP_BIND     174    175       GTP. {ECO:0000256|HAMAP-Rule:MF_03169}.
FT   REGION       42     71       NMPbind. {ECO:0000256|HAMAP-Rule:
FT                                MF_03169}.
FT   REGION      164    201       LID. {ECO:0000256|HAMAP-Rule:MF_03169}.
FT   BINDING      43     43       AMP. {ECO:0000256|HAMAP-Rule:MF_03169}.
FT   BINDING      48     48       AMP. {ECO:0000256|HAMAP-Rule:MF_03169}.
FT   BINDING     135    135       AMP. {ECO:0000256|HAMAP-Rule:MF_03169}.
FT   BINDING     165    165       GTP. {ECO:0000256|HAMAP-Rule:MF_03169}.
FT   BINDING     198    198       AMP. {ECO:0000256|HAMAP-Rule:MF_03169}.
FT   BINDING     209    209       AMP. {ECO:0000256|HAMAP-Rule:MF_03169}.
FT   BINDING     238    238       GTP; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03169}.
SQ   SEQUENCE   254 AA;  28052 MW;  8269449CF828B7C3 CRC64;
     MSHTTKQLRK AARIILIGAP GVGKGTQSER LLARFPQLVS ISSGDLLREN VRRRTPLGLE
     AEAAMQSGNL VPDSMILNLI SDDMKSKGWL LPPRTSSVQP TASSSSSSLA DTSSSHSIDS
     SASFILDGFP RTATQAATLD SLVPVNFVVH LITPPSVILA RIASRWVHEP SGRVYNTDFH
     PPKVPGKDDV TGEPLTQRED DSLETWKQRL RKFEETSKSL LEHYDRQRCL FRAEGNSSDE
     ISPKLFAEVE RRFC
//

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