ID M3BZT2_STRMB Unreviewed; 1232 AA.
AC M3BZT2;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=H340_27342 {ECO:0000313|EMBL:EME97260.1};
OS Streptomyces mobaraensis NBRC 13819 = DSM 40847.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1223523 {ECO:0000313|EMBL:EME97260.1, ECO:0000313|Proteomes:UP000011740};
RN [1] {ECO:0000313|EMBL:EME97260.1, ECO:0000313|Proteomes:UP000011740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40847 {ECO:0000313|EMBL:EME97260.1,
RC ECO:0000313|Proteomes:UP000011740};
RX PubMed=23558536;
RA Yang H., He T., Wu W., Zhu W., Lu B., Sun W.;
RT "Whole-Genome Shotgun Assembly and Analysis of the Genome of Streptomyces
RT mobaraensis DSM 40847, a Strain for Industrial Production of Microbial
RT Transglutaminase.";
RL Genome Announc. 1:E0014313-E0014313(2013).
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 -!- 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:EME97260.1}.
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DR EMBL; AORZ01000132; EME97260.1; -; Genomic_DNA.
DR AlphaFoldDB; M3BZT2; -.
DR STRING; 1223523.H340_27342; -.
DR PATRIC; fig|1223523.3.peg.5555; -.
DR eggNOG; COG0125; Bacteria.
DR Proteomes; UP000011740; 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; IPR018095; Thymidylate_kin_CS.
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.
DR PROSITE; PS01331; THYMIDYLATE_KINASE; 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:EME97260.1};
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}; Transferase {ECO:0000256|HAMAP-Rule:MF_00165};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 34..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 68..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 134..153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 194..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 227..248
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 283..307
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 313..334
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 346..364
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 370..392
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 412..433
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 445..466
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 503..687
FT /note="Thymidylate kinase-like"
FT /evidence="ECO:0000259|Pfam:PF02223"
FT REGION 748..1232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..839
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..960
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1117..1165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1173..1203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 505..512
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00165"
SQ SEQUENCE 1232 AA; 128120 MW; 78294EEDAA0CCD02 CRC64;
MTSPSGALAA DSRERAVRAL LRIPSLRRLW SAQAAGGVGD ALGLLVLLLL ALQAAVTAGS
FGGGYRGAAF AVAAVLGARL LATLLLGTVL LGPFNALLAP SGPLDRRWTM IGADAVRALL
LAVAPVWIDF TESKALASLL VTAFLLGVAE RVWTVAKDGV APTLLPRPPL EGAAVRPVPD
HGDALRRLTL RTSFVALPAA AAALVAVTLV SNLLGSGIDW FHQHQPALGS YLAAALFNAS
GVIVYFLALP AAREVTARSP LEGLRRPKRD QAPDKGRTGG IPVFVLSCAA VAGAVAAAFG
VAVLQAYDLG GGPVAFGLLA LALTGGPVLG IRSAGRVLPG FSRRRLLALS LAVTGVALLA
AGLVPDATTV LLLILVAGVS AGVVANTGHA LLDQEAEEER RPGVTEHLHA VVRVTVAPAA
VVAPVLAALI GPHRAESGNF VFDHGGAAFT LMLIGALLLP VGALVLGKTD DRHGVPFHRD
LLDAVRDGDP VEATAADGFF LVFDGGDGAG KSTQVQAIAE WIRSKGHEVV VTREPGATAI
GKRLRAILLD VASAGLSDRA EALLYAADRA EHINAVVRPA LERGAVVISD RYIDSSVAYQ
GAGRDLSPTE IARINRWATE GLVPHLTVLL DVSPETARER FTEAPDRLES EPAEFHERVR
KGFLALAAAD PARYLVVDAG QEPEAVTTVV RHRLDEVLPL SAQEIEAREA ARRAAEAEAR
RKAEEEAARK AEEERLERER QERLAKLRAE EEERKRREAE EARRLEAERQ AEEARQRAEE
ARRLADEERR RREAEDRARA AEQERLRKQA EEEARLRAEA EERRREKQRK AEEALLRAEA
ARTAGDGAAA DGAAGDGVAA AEGASADGAP GIGAGARAAA GADEAPTVER SALRESGAEG
AAGAGAAGKA ADLTKRATAS DAGSAAPRAG ARAADAERTE QLRVPPVHRP DPRESLLMRD
ADETVTVQSP LVHRKDPHEA DRAAGGEAVS GEAGAEDETA VLPTTGPAGA GKAKAVGGKG
ASGEAAAEDE TAVLPTTGST RSGKASVGAE DETAYLPPVR SDGPASAGAP EAAEDETTVL
PPVPTLPPPV QRVTWGLRSG KNDADGAETA GPTDAGRAED PVERVPDWLF RPEESAGTDR
PGGAEGERTP ADDADGMRTR EMPRPGAEAD AAGAAERARK ARRRPEWAEG DREGDDAEAP
TLADDLFGRR AGGSGDGPDG GASGAPGRRG GR
//
