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Database: UniProt/SWISS-PROT
Entry: KITH_CLOAB
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Original site: KITH_CLOAB 
ID   KITH_CLOAB              Reviewed;         195 AA.
AC   Q97F65;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   07-JUN-2017, entry version 98.
DE   RecName: Full=Thymidine kinase {ECO:0000255|HAMAP-Rule:MF_00124};
DE            EC=2.7.1.21 {ECO:0000255|HAMAP-Rule:MF_00124};
GN   Name=tdk {ECO:0000255|HAMAP-Rule:MF_00124};
GN   OrderedLocusNames=CA_C2887;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG
OS   5710 / VKM B-1787).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=11466286; DOI=10.1128/JB.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q.,
RA   Gibson R., Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I.,
RA   Tatusov R.L., Sabathe F., Doucette-Stamm L.A., Soucaille P.,
RA   Daly M.J., Bennett G.N., Koonin E.V., Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-191 IN COMPLEX WITH ZINC
RP   IONS AND ADP.
RG   Northeast structural genomics consortium (NESG);
RT   "X-ray structure of clostridium acetobutylicum genomics target
RT   CAR26.";
RL   Submitted (FEB-2009) to the PDB data bank.
CC   -!- CATALYTIC ACTIVITY: ATP + thymidine = ADP + thymidine 5'-
CC       phosphate. {ECO:0000255|HAMAP-Rule:MF_00124}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00124}.
CC   -!- SIMILARITY: Belongs to the thymidine kinase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00124}.
DR   EMBL; AE001437; AAK80830.1; -; Genomic_DNA.
DR   PIR; C97255; C97255.
DR   RefSeq; NP_349490.1; NC_003030.1.
DR   RefSeq; WP_010966171.1; NC_003030.1.
DR   PDB; 1XX6; X-ray; 2.00 A; A/B=1-191.
DR   PDBsum; 1XX6; -.
DR   ProteinModelPortal; Q97F65; -.
DR   SMR; Q97F65; -.
DR   STRING; 272562.CA_C2887; -.
DR   EnsemblBacteria; AAK80830; AAK80830; CA_C2887.
DR   GeneID; 1119070; -.
DR   KEGG; cac:CA_C2887; -.
DR   PATRIC; fig|272562.8.peg.3071; -.
DR   eggNOG; ENOG4107104; Bacteria.
DR   eggNOG; COG1435; LUCA.
DR   HOGENOM; HOG000076390; -.
DR   KO; K00857; -.
DR   OMA; CAGLDQD; -.
DR   BRENDA; 2.7.1.21; 1452.
DR   EvolutionaryTrace; Q97F65; -.
DR   Proteomes; UP000000814; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004797; F:thymidine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR   HAMAP; MF_00124; Thymidine_kinase; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001267; Thymidine_kinase.
DR   InterPro; IPR020633; Thymidine_kinase_CS.
DR   PANTHER; PTHR11441; PTHR11441; 1.
DR   Pfam; PF00265; TK; 1.
DR   PIRSF; PIRSF035805; TK_cell; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00603; TK_CELLULAR_TYPE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Complete proteome; Cytoplasm;
KW   DNA synthesis; Kinase; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Transferase; Zinc.
FT   CHAIN         1    195       Thymidine kinase.
FT                                /FTId=PRO_0000174967.
FT   NP_BIND      15     22       ATP.
FT   NP_BIND      57     58       ATP.
FT   NP_BIND      88     91       ATP. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   ACT_SITE     89     89       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00124}.
FT   METAL       145    145       Zinc.
FT   METAL       148    148       Zinc.
FT   METAL       183    183       Zinc.
FT   METAL       186    186       Zinc.
FT   BINDING      23     23       ATP.
FT   BINDING     120    120       Substrate; via amide nitrogen.
FT                                {ECO:0000250}.
FT   BINDING     179    179       Substrate. {ECO:0000250}.
FT   STRAND        9     14       {ECO:0000244|PDB:1XX6}.
FT   HELIX        21     34       {ECO:0000244|PDB:1XX6}.
FT   STRAND       39     44       {ECO:0000244|PDB:1XX6}.
FT   STRAND       54     56       {ECO:0000244|PDB:1XX6}.
FT   STRAND       62     64       {ECO:0000244|PDB:1XX6}.
FT   STRAND       66     71       {ECO:0000244|PDB:1XX6}.
FT   HELIX        73     77       {ECO:0000244|PDB:1XX6}.
FT   STRAND       83     87       {ECO:0000244|PDB:1XX6}.
FT   HELIX        90     92       {ECO:0000244|PDB:1XX6}.
FT   HELIX        97    106       {ECO:0000244|PDB:1XX6}.
FT   STRAND      110    115       {ECO:0000244|PDB:1XX6}.
FT   HELIX       128    134       {ECO:0000244|PDB:1XX6}.
FT   STRAND      136    140       {ECO:0000244|PDB:1XX6}.
FT   TURN        146    148       {ECO:0000244|PDB:1XX6}.
FT   STRAND      149    152       {ECO:0000244|PDB:1XX6}.
FT   STRAND      154    159       {ECO:0000244|PDB:1XX6}.
FT   STRAND      177    182       {ECO:0000244|PDB:1XX6}.
FT   TURN        184    186       {ECO:0000244|PDB:1XX6}.
SQ   SEQUENCE   195 AA;  22303 MW;  6EDB551986B203BA CRC64;
     MYRPKDHGWV EVIVGPMYSG KSEELIRRIR RAKIAKQKIQ VFKPEIDNRY SKEDVVSHMG
     EKEQAVAIKN SREILKYFEE DTEVIAIDEV QFFDDEIVEI VNKIAESGRR VICAGLDMDF
     RGKPFGPIPE LMAIAEFVDK IQAICVVCGN PATRTQRLIN GKPAFYDDPV VLIGAMESYE
     ARCRKCHVVP QKKEV
//
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