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Entry: A0A087BNM8_9BIFI
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ID   A0A087BNM8_9BIFI        Unreviewed;       595 AA.
AC   A0A087BNM8;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Cytidylate kinase {ECO:0000256|HAMAP-Rule:MF_00238};
DE            Short=CK {ECO:0000256|HAMAP-Rule:MF_00238};
DE            EC=2.7.4.25 {ECO:0000256|HAMAP-Rule:MF_00238};
DE   AltName: Full=Cytidine monophosphate kinase {ECO:0000256|HAMAP-Rule:MF_00238};
DE            Short=CMP kinase {ECO:0000256|HAMAP-Rule:MF_00238};
GN   Name=cmk {ECO:0000256|HAMAP-Rule:MF_00238};
GN   ORFNames=BMIN_0526 {ECO:0000313|EMBL:KFI72628.1};
OS   Bifidobacterium minimum.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1693 {ECO:0000313|EMBL:KFI72628.1, ECO:0000313|Proteomes:UP000029014};
RN   [1] {ECO:0000313|EMBL:KFI72628.1, ECO:0000313|Proteomes:UP000029014}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 11592 {ECO:0000313|EMBL:KFI72628.1,
RC   ECO:0000313|Proteomes:UP000029014};
RA   Ventura M., Milani C., Lugli G.A.;
RT   "Genomics of Bifidobacteria.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377,
CC         ChEBI:CHEBI:456216; EC=2.7.4.25;
CC         Evidence={ECO:0000256|ARBA:ARBA00001097, ECO:0000256|HAMAP-
CC         Rule:MF_00238};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593,
CC         ChEBI:CHEBI:456216; EC=2.7.4.25;
CC         Evidence={ECO:0000256|ARBA:ARBA00001115, ECO:0000256|HAMAP-
CC         Rule:MF_00238};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00238}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC       GTPase superfamily. EngA (Der) GTPase family.
CC       {ECO:0000256|ARBA:ARBA00008279, ECO:0000256|PROSITE-ProRule:PRU01049}.
CC   -!- SIMILARITY: Belongs to the cytidylate kinase family. Type 1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00009427, ECO:0000256|HAMAP-Rule:MF_00238}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KFI72628.1}.
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DR   EMBL; JGZD01000009; KFI72628.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A087BNM8; -.
DR   STRING; 1693.BMIN_0526; -.
DR   eggNOG; COG0283; Bacteria.
DR   eggNOG; COG1160; Bacteria.
DR   Proteomes; UP000029014; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0036430; F:CMP kinase activity; IEA:RHEA.
DR   GO; GO:0036431; F:dCMP kinase activity; IEA:RHEA.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006220; P:pyrimidine nucleotide metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR   CDD; cd02020; CMPK; 1.
DR   CDD; cd01894; EngA1; 1.
DR   CDD; cd01895; EngA2; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   HAMAP; MF_00238; Cytidyl_kinase_type1; 1.
DR   InterPro; IPR003136; Cytidylate_kin.
DR   InterPro; IPR011994; Cytidylate_kinase_dom.
DR   InterPro; IPR031166; G_ENGA.
DR   InterPro; IPR006073; GTP-bd.
DR   InterPro; IPR016484; GTPase_Der.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   NCBIfam; TIGR03594; GTPase_EngA; 1.
DR   NCBIfam; TIGR00231; small_GTP; 2.
DR   PANTHER; PTHR43834; GTPASE DER; 1.
DR   PANTHER; PTHR43834:SF6; GTPASE DER; 1.
DR   Pfam; PF02224; Cytidylate_kin; 1.
DR   Pfam; PF01926; MMR_HSR1; 2.
DR   PRINTS; PR00326; GTP1OBG.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR   PROSITE; PS51712; G_ENGA; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00238};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00238};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00238, ECO:0000313|EMBL:KFI72628.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00238};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029014};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00238, ECO:0000313|EMBL:KFI72628.1}.
FT   DOMAIN          273..436
FT                   /note="EngA-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51712"
FT   BINDING         8..16
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00238"
SQ   SEQUENCE   595 AA;  64087 MW;  A38AEA52BCD46A84 CRC64;
     MIRVAIDGPA GVGKSSTSKA LAEHYGYAYL DTGAMYRACA WWCIRSGLDL DAEDLDAQAI
     TEAVGDFFTG GHARFGVDPK DPVVESDGRD IRDEIRSHDV SSHVSTVSSI IPVRHVLIAA
     QRAIIAQESD AESFSHGTGI VVEGRDITTV VAPDAEVRVL LTAREDVRQA RRSGQKSAGV
     GQDDVAARDH ADSTVTSFLS AADGVTTVDN SDLTFQQTLD ALIALVDAAI DEQEYQRYAA
     NLEGYDLDDD DRRLLDGDES RDAAGTASAR MVGVIAVVGR PNVGKSTLVN RILGRRAAVV
     EDVPGVTRDR VSYDAEWAGT DFRLVDTGGW ESGVEGIDSA VADQAEIAVG LADTVILVVD
     GQVGMTATDE RIVSMLRASG KTVTLAVNKI DGQSAEYLTA EFWKLGMGQP YGISAMHGRG
     IGELLDAAVA ALSRSSRTSG SLTPSHLRRV ALIGRPNVGK SSLLNQMAHN ERSVVNELAG
     TTRDPVDDVV TIDGEDWLFI DTAGIRRRQH KLTGAEYYSS LRTAAAIDRA ELVLVLFDAS
     QPISDQDLKV MSQAVDAGRA VVLVFNKWDL ADEFVRQRVE RLWQTEFDRV TWLNA
//
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