ID D4YMX5_9MICO Unreviewed; 824 AA.
AC D4YMX5;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 18-SEP-2019, entry version 49.
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 ECO:0000313|EMBL:EFG47440.1};
GN ORFNames=HMPREF0183_1232 {ECO:0000313|EMBL:EFG47440.1};
OS Brevibacterium mcbrellneri ATCC 49030.
OC Bacteria; Actinobacteria; Micrococcales; Brevibacteriaceae;
OC Brevibacterium.
OX NCBI_TaxID=585530 {ECO:0000313|EMBL:EFG47440.1, ECO:0000313|Proteomes:UP000005714};
RN [1] {ECO:0000313|EMBL:EFG47440.1, ECO:0000313|Proteomes:UP000005714}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49030 {ECO:0000313|EMBL:EFG47440.1,
RC ECO:0000313|Proteomes:UP000005714};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C.,
RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L.,
RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y.,
RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L.,
RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F.,
RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M.,
RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S.,
RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J.,
RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J.,
RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D.,
RA Worley K., Gibbs R.;
RL Submitted (APR-2010) 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-
CC 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; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00165, ECO:0000256|SAAS:SAAS01114966};
CC -!- SIMILARITY: Belongs to the thymidylate kinase family.
CC {ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000256|SAAS:SAAS01070220}.
CC -!- CAUTION: The sequence shown here is derived from an
CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC preliminary data. {ECO:0000313|EMBL:EFG47440.1}.
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DR EMBL; ADNU01000037; EFG47440.1; -; Genomic_DNA.
DR RefSeq; WP_005883937.1; NZ_ADNU01000037.1.
DR STRING; 585530.HMPREF0183_1232; -.
DR EnsemblBacteria; EFG47440; EFG47440; HMPREF0183_1232.
DR eggNOG; ENOG4108ZMD; Bacteria.
DR eggNOG; COG0125; LUCA.
DR OrthoDB; 257682at2; -.
DR BioCyc; GCF_000178455-HMP:HMPREF0183_RS12095-MONOMER; -.
DR Proteomes; UP000005714; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of 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 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 Pfam; PF02223; Thymidylate_kin; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00041; DTMP_kinase; 1.
DR PROSITE; PS01331; THYMIDYLATE_KINASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00165,
KW ECO:0000256|SAAS:SAAS01070209};
KW Complete proteome {ECO:0000313|Proteomes:UP000005714};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00165,
KW ECO:0000256|SAAS:SAAS01070206, ECO:0000313|EMBL:EFG47440.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00165,
KW ECO:0000256|SAAS:SAAS01070211};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00165,
KW ECO:0000256|SAAS:SAAS01070205};
KW Reference proteome {ECO:0000313|Proteomes:UP000005714};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00165,
KW ECO:0000256|SAAS:SAAS01070204, ECO:0000313|EMBL:EFG47440.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 24 45 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 65 87 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 99 118 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 124 145 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 152 170 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 182 204 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 234 254 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 266 285 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 297 315 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 347 366 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 378 403 Helical. {ECO:0000256|SAM:Phobius}.
FT DOMAIN 479 667 Thymidylate_kin. {ECO:0000259|Pfam:
FT PF02223}.
FT NP_BIND 481 488 ATP. {ECO:0000256|HAMAP-Rule:MF_00165}.
FT REGION 701 824 Disordered. {ECO:0000256|SAM:MobiDB-
FT lite}.
FT COMPBIAS 707 721 Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT lite}.
FT COMPBIAS 780 800 Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT lite}.
SQ SEQUENCE 824 AA; 87222 MW; ABB652D20A6B222D CRC64;
MDTQTVLSKP HAGTIGHAAL EVGAWLVALS SAAISFAIVG IHGFGGAMDI SRYGELTQIQ
RDGGFNSSFA VPGLLAFFAL AVAGVLIPPK KLTQLKESVR SQLLTLFAAA TACVSVVVVF
IPTFWLTLIV AALLGMLVGV LAAHAPELHT KPWRTGGLAV GIFLLVTYYF ELEHGVPAGA
HALRWLLFVG AILLIVAALM VLVFPLSSDR DIDDLHTFPH TLAIKRSRGH MSIAFPWACY
ALFAVLGALF LLPLPATVDG GYGQGAIGLM TAAVLLGWAA GYESGPTFAP GMTRPRLTAF
ALVAAGLLMI CAGLIDELSG KAVLMALTAF CVGVGVRAQK YEFSRRVGLA VGALLATLLC
GLDLTFDIHL SAVTTWVLSA SGVAFSAIGL LAFATGILAI FFFSPMGVRG MGVDLMNAFQ
VSGDSSPRAT APAFAVAEDQ ETRVLPAATT SADEPQDAGA NYLAVPEPVT PSTGLFIAIE
GGDGAGKTTQ IRKLVEHLES RGFDPVIATR EPGGTPVGKS IRSVLLDGEA VSKKSEALLY
AADRAHHVAT LVAPSLEQDG AVVTDRYIDS SLAYQAGGRE LSEDDVLALS RWATSGLVPN
LTLVLDIDPR VAAERMGNRE DANHLDKQSL EFKDRVRAGF LRLAEAEPDR YAVIPAGRSV
NEVAEHIQRV VDAIIDGEES ADVADTFEPI APRGVFVGVP TERMSPEDAQ KAVDEHRYAE
SPQFLTEPIK ADGAEDADSA ASAESTEDTE NAATTVLPQR PKAEGAPKPG GPTRAQAEPE
TPETQEKPTD TAEPDPETYR AKLQRQSMIE QQARQRLRDA RRNS
//
