ID A0A1H7PVI9_STRJI Unreviewed; 1271 AA.
AC A0A1H7PVI9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Thymidylate kinase {ECO:0000256|HAMAP-Rule:MF_00165};
DE EC=2.7.4.9 {ECO:0000256|HAMAP-Rule:MF_00165};
DE AltName: Full=dTMP kinase {ECO:0000256|HAMAP-Rule:MF_00165};
GN Name=tmk {ECO:0000256|HAMAP-Rule:MF_00165};
GN ORFNames=SAMN05414137_108153 {ECO:0000313|EMBL:SEL39850.1};
OS Streptacidiphilus jiangxiensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptacidiphilus.
OX NCBI_TaxID=235985 {ECO:0000313|EMBL:SEL39850.1, ECO:0000313|Proteomes:UP000183015};
RN [1] {ECO:0000313|Proteomes:UP000183015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45096 / BCRC 16803 / CGMCC 4.1857 / CIP 109030 / JCM 12277
RC / KCTC 19219 / NBRC 100920 / 33214
RC {ECO:0000313|Proteomes:UP000183015};
RA Varghese N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and
CC salvage pathways of dTTP synthesis. {ECO:0000256|HAMAP-Rule:MF_00165}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528,
CC ChEBI:CHEBI:456216; EC=2.7.4.9;
CC Evidence={ECO:0000256|ARBA:ARBA00001008, ECO:0000256|HAMAP-
CC Rule:MF_00165};
CC -!- SIMILARITY: Belongs to the thymidylate kinase family.
CC {ECO:0000256|ARBA:ARBA00009776, ECO:0000256|HAMAP-Rule:MF_00165}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FOAZ01000008; SEL39850.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7PVI9; -.
DR STRING; 235985.SAMN05414137_108153; -.
DR eggNOG; COG0125; Bacteria.
DR OrthoDB; 9774907at2; -.
DR Proteomes; UP000183015; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004798; F:thymidylate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006233; P:dTDP biosynthetic process; IEA:InterPro.
DR GO; GO:0006235; P:dTTP biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01672; TMPK; 1.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00165; Thymidylate_kinase; 1.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039430; Thymidylate_kin-like_dom.
DR InterPro; IPR018094; Thymidylate_kinase.
DR NCBIfam; TIGR00041; DTMP_kinase; 1.
DR PANTHER; PTHR10344; THYMIDYLATE KINASE; 1.
DR PANTHER; PTHR10344:SF4; THYMIDYLATE KINASE; 1.
DR Pfam; PF02223; Thymidylate_kin; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00165};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000313|EMBL:SEL39850.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00165};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00165}; Reference proteome {ECO:0000313|Proteomes:UP000183015};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00165};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 60..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 85..112
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 150..168
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 202..221
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 233..254
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 300..322
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 334..352
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 364..382
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 388..407
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 428..449
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 464..485
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 523..710
FT /note="Thymidylate kinase-like"
FT /evidence="ECO:0000259|Pfam:PF02223"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 774..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 838..1271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..791
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..822
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..860
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1085..1108
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1252..1271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 525..532
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00165"
SQ SEQUENCE 1271 AA; 132991 MW; 20713B0A5E69B80C CRC64;
MSAESQEPTS EAPESPTPQD RSSGASVGVS PTDRARALLR GRAYGRAWRA QAVGTLGDRL
ALLTLLVLTV RAVIGAQALS GGYAATLFAL AAAFGARLLG TLLFGAVLLS PLAQLTRRLD
RRQLLLGAEA ARAALLGCSL FWVTWAGTRA WIWLLVTVFL TATLERVVTV TRESFAEALL
PSAAPGHPAV DQRPVLRHID LWTGYVAIPL AALGFIVMML LNQGVGQGVA WLSAHPLALS
GFGAAALFVF AGVLHFRQEL PDADTEGARS FEPRSPLTNL RAPADVTPGL GARGRTGSSL
TFSFAACSTA AAIAAAAAVA YVHALDLLAG EIGFGLLVLA LTAGLLLGLR VSRSVLPPLS
RRRLLPLAMV VAGLGLVLGG LVRDYVLALV LFSLAGIAGG VAFRGARDLL RQETEEARQP
KVDEHLHAML RVAVALALLA SPLIGAAFGP EQFGGTTLTF DHGGAGLAVA LAGLLLVIAG
VVVLLRADDR KGVAPLPRDV WDALTAGSER PAYRAGTGFF IALEGGDGAG KSTQAQALAE
WIRSKGHEVV LTREPGGSAI GQRLRAMLLD VANTGISHRA EALIFAADRA EHVDSVILPA
LERGAVVITD RYMDSSISYQ GAGRDLAAAD IARLNRWATG GLVPDLTVVL DVAPSAARER
FTDAPDRMES EPEAFHQRVR SAFLALAAAD PARYLIVDAG RPPHAVTTSI RHRLDRELPL
SEQEKAALAE RERLAREAEA RRLEEEARRK AEEERAERER QAMLERLRLE AEEAEKARQA
EEDRKAAEAA RQAAEAARAA AEAEAARRAE EEAERRRAEE AARVAALAEA ARLAELERQR
AEKRAEERRR AEEALQRAEE SRLAAEAAAA AAAAAAGAAG ADARASESRD GGADHIATAR
GESAPRSAAA DETAVLPRVP ATAEDDDADG VAATAELPRF DPTRSGASDG ASDRTAVLPR
VTDATPAPDA VESTAELPRF AGADTGAAAA DETAVLPRVV EGSRADDAAG RDAARESGAS
GGPTKAAPDT GVGTDTDTGT TAEREVEKTA ALPVVDAGAG PRAARAPKST PGVAGGAADE
TMVLPPMPAR PPVVGGPTSL PAPVEPEAPK KPRLPRFGRK AAGQPEGSAD AAVTPAPAAD
ETAVLPVVEP GAQQPLPRSW REAAPRSSES VQDRVPDWLF RPEQGPAGSE APTTQIPPVA
QIPSVPQNPA VEPDVEATPS RGGRYDWAEE TPLDDLPSLT DQLLGTREEW AQWHSDNPDE
EQGPGGHGRR G
//
