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Database: UniProt
Entry: D0F7V7_9VIBR
LinkDB: D0F7V7_9VIBR
Original site: D0F7V7_9VIBR 
ID   D0F7V7_9VIBR            Unreviewed;       135 AA.
AC   D0F7V7;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=Adenylate kinase {ECO:0000256|RuleBase:RU003331};
DE            EC=2.7.4.3 {ECO:0000256|RuleBase:RU003331};
DE   Flags: Fragment;
GN   Name=adk {ECO:0000313|EMBL:ACX58390.1};
OS   Vibrio sp. 0407MHC76.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=677165 {ECO:0000313|EMBL:ACX58390.1};
RN   [1] {ECO:0000313|EMBL:ACX58390.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=0407MHC76 {ECO:0000313|EMBL:ACX58390.1};
RX   PubMed=20819104; DOI=10.1111/j.1462-2920.2010.02328.x;
RA   Preheim S.P., Boucher Y., Wildschutte H., David L.A., Veneziano D.,
RA   Alm E.J., Polz M.F.;
RT   "Metapopulation structure of Vibrionaceae among coastal marine
RT   invertebrates.";
RL   Environ. Microbiol. 13:265-275(2011).
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:0000256|ARBA:ARBA00000582,
CC         ECO:0000256|RuleBase:RU003331};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245,
CC       ECO:0000256|RuleBase:RU003331}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|RuleBase:RU003331}.
CC   -!- SIMILARITY: Belongs to the adenylate kinase family.
CC       {ECO:0000256|ARBA:ARBA00007220, ECO:0000256|RuleBase:RU003330}.
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DR   EMBL; GQ990891; ACX58390.1; -; Genomic_DNA.
DR   AlphaFoldDB; D0F7V7; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004017; F:adenylate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd01428; ADK; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00235; Adenylate_kinase_Adk; 1.
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; NUCLEOTIDE KINASE; 1.
DR   PANTHER; PTHR23359:SF206; UMP-CMP KINASE; 1.
DR   Pfam; PF00406; ADK; 1.
DR   Pfam; PF05191; ADK_lid; 1.
DR   PRINTS; PR00094; ADENYLTKNASE.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003331};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU003330};
KW   Nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022727};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU003331};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003330}.
FT   DOMAIN          91..126
FT                   /note="Adenylate kinase active site lid"
FT                   /evidence="ECO:0000259|Pfam:PF05191"
FT   REGION          96..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..135
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACX58390.1"
FT   NON_TER         135
FT                   /evidence="ECO:0000313|EMBL:ACX58390.1"
SQ   SEQUENCE   135 AA;  14942 MW;  088171AFD5DDF3DB CRC64;
     DMLRAAIKAG TELGKQAKSV IDAGQLVSDE IILGLIKERI AQDDCEKGFL LDGFPRTIPQ
     ADGLKEMGIA VDYVVEFDVA DDVIVERMTG RRAHLPSGRT YHSVYNPPKE EGKDDITGEE
     LVVRDDDKEE TVRAR
//
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