KADC_MAIZE
ID KADC_MAIZE Reviewed; 222 AA.
AC P43188;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Adenylate kinase, chloroplastic;
DE Short=AK;
DE EC=2.7.4.3 {ECO:0000269|PubMed:16664952};
DE AltName: Full=ATP-AMP transphosphorylase;
DE AltName: Full=ATP:AMP phosphotransferase;
DE AltName: Full=Adenylate monophosphate kinase;
GN Name=ADK1;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
RC TISSUE=Leaf;
RX PubMed=8026505; DOI=10.1111/j.1432-1033.1994.tb18944.x;
RA Schiltz E., Burger S., Grafmueller R., Deppert W.R., Haehnel W., Wagner E.;
RT "Primary structure of maize chloroplast adenylate kinase.";
RL Eur. J. Biochem. 222:949-954(1994).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=4309527; DOI=10.1042/bj1140489;
RA Slack C.R., Hatch M.D., Goodchild D.J.;
RT "Distribution of enzymes in mesophyll and parenchyma-sheath chloroplasts of
RT maize leaves in relation to the C4-dicarboxylic acid pathway of
RT photosynthesis.";
RL Biochem. J. 114:489-498(1969).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND SUBUNIT.
RX PubMed=16664952; DOI=10.1104/pp.81.4.1110;
RA Kleczkowski L.A., Randall D.D.;
RT "Maize leaf adenylate kinase: purification and partial characterization.";
RL Plant Physiol. 81:1110-1114(1986).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) IN COMPLEX WITH BI-SUBSTRATE ANALOG
RP AP5A.
RX PubMed=9428681; DOI=10.1111/j.1432-1033.1997.0326a.x;
RA Wild K., Grafmueller R., Wagner E., Schulz G.E.;
RT "Structure, catalysis and supramolecular assembly of adenylate kinase from
RT maize.";
RL Eur. J. Biochem. 250:326-331(1997).
CC -!- FUNCTION: Catalyzes the reversible transfer of the terminal phosphate
CC group between ATP and AMP. Plays an important role in cellular energy
CC homeostasis and in adenine nucleotide metabolism. The maize enzyme also
CC works with CMP, albeit with 10% of the activity with AMP.
CC {ECO:0000269|PubMed:16664952}.
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:0000269|PubMed:16664952};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16664952}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:4309527}.
CC -!- MASS SPECTROMETRY: Mass=24867; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8026505};
CC -!- SIMILARITY: Belongs to the adenylate kinase family. {ECO:0000305}.
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DR PIR; S45634; S45634.
DR PDB; 1ZAK; X-ray; 3.50 A; A/B=1-222.
DR PDBsum; 1ZAK; -.
DR AlphaFoldDB; P43188; -.
DR SMR; P43188; -.
DR STRING; 4577.GRMZM2G178192_P03; -.
DR PaxDb; P43188; -.
DR PRIDE; P43188; -.
DR MaizeGDB; 13836; -.
DR eggNOG; KOG3078; Eukaryota.
DR EvolutionaryTrace; P43188; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; P43188; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004017; F:adenylate kinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004127; F:cytidylate kinase activity; IBA:GO_Central.
DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IBA:GO_Central.
DR GO; GO:0006165; P:nucleoside diphosphate phosphorylation; IBA:GO_Central.
DR GO; GO:0009142; P:nucleoside triphosphate biosynthetic process; IBA:GO_Central.
DR CDD; cd01428; ADK; 1.
DR Gene3D; 3.40.50.300; -; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chloroplast; Direct protein sequencing; Kinase;
KW Nucleotide-binding; Plastid; Reference proteome; Transferase.
FT CHAIN 1..222
FT /note="Adenylate kinase, chloroplastic"
FT /id="PRO_0000158939"
FT REGION 35..64
FT /note="NMP"
FT /evidence="ECO:0000269|PubMed:9428681"
FT REGION 128..161
FT /note="LID"
FT /evidence="ECO:0000269|PubMed:9428681"
FT BINDING 15..20
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:9428681"
FT BINDING 41
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:9428681"
FT BINDING 62..64
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:9428681"
FT BINDING 91..94
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:9428681"
FT BINDING 98
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:9428681"
FT BINDING 129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:9428681"
FT BINDING 158
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:9428681"
FT BINDING 195
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:9428681"
FT STRAND 8..13
FT /evidence="ECO:0007829|PDB:1ZAK"
FT HELIX 18..29
FT /evidence="ECO:0007829|PDB:1ZAK"
FT HELIX 36..46
FT /evidence="ECO:0007829|PDB:1ZAK"
FT HELIX 49..59
FT /evidence="ECO:0007829|PDB:1ZAK"
FT HELIX 66..78
FT /evidence="ECO:0007829|PDB:1ZAK"
FT HELIX 80..84
FT /evidence="ECO:0007829|PDB:1ZAK"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:1ZAK"
FT HELIX 96..103
FT /evidence="ECO:0007829|PDB:1ZAK"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:1ZAK"
FT STRAND 110..116
FT /evidence="ECO:0007829|PDB:1ZAK"
FT HELIX 119..126
FT /evidence="ECO:0007829|PDB:1ZAK"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:1ZAK"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:1ZAK"
FT STRAND 138..144
FT /evidence="ECO:0007829|PDB:1ZAK"
FT HELIX 150..154
FT /evidence="ECO:0007829|PDB:1ZAK"
FT HELIX 165..182
FT /evidence="ECO:0007829|PDB:1ZAK"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:1ZAK"
FT HELIX 197..219
FT /evidence="ECO:0007829|PDB:1ZAK"
SQ SEQUENCE 222 AA; 24867 MW; 19257324F8B7630D CRC64;
ALADPLKVMI SGAPASGKGT QCELIKTKYQ LAHISAGDLL RAEIAAGSEN GKRAKEFMEK
GQLVPDEIVV NMVKERLRQP DAQENGWLLD GYPRSYSQAM ALETLEIRPD TFILLDVPDE
LLVERVVGRR LDPVTGKIYH LKYSPPENEE IASRLTQRFD DTEEKVKLRL ETYYQNIESL
LSTYENIIVK VQGDATVDAV FAKIDELLGS ILEKKNEMVS ST
