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⊟Summary[edit | edit source]
- pan ID?: SAUPAN003859000
- symbol?: thyA
- synonym:
- description?: thymidylate synthase
- strand?: -
- coordinates?: 4140366..4141322
- synteny block?: BlockID0029150
- occurrence?: in 100% of 34 strains
thyA : thymidylate synthase [1]
• A crystal structure is available : 4DQ1
Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.
⊟Orthologs[edit | edit source]
04-02981:
SA2981_1381 (thyA)
08BA02176:
C248_1467 (thyA)
11819-97:
MS7_1383 (thyA)
6850:
RSAU_001306 (thyA)
71193:
ST398NM01_1428
ECT-R 2:
ECTR2_1283 (thyA)
ED133:
SAOV_1436c
ED98:
SAAV_1410 (thyA)
HO 5096 0412:
SAEMRSA15_12900 (thyA)
JH1:
SaurJH1_1516 (thyA)
JH9:
SaurJH9_1487 (thyA)
JKD6008:
SAA6008_01395 (thyA)
JKD6159:
SAA6159_01294 (thyA)
JSNZ:
JSNZ_001412
LGA251:
SARLGA251_13430 (thyA)
M013:
M013TW_1373
MRSA252:
SAR1440 (thyA)
MSHR1132:
SAMSHR1132_12690
MSSA476:
SAS1370 (thyA)
Mu3:
SAHV_1415 (thyA)
Mu50:
SAV1427 (thyA)
MW2:
MW1317 (thyA)
RF122:
SAB1282c (thyA)
ST398:
SAPIG1428 (thyA)
T0131:
SAT0131_01507 (guaA)
TCH60:
HMPREF0772_11779 (thyA)
TW20:
SATW20_14280 (thyA)
USA300_TCH1516:
USA300HOU_1364 (thyA)
VC40:
SAVC_06385 (thyA)
⊟Genome Viewer[edit | edit source]
| COL | |
| N315 | |
| NCTC8325 | |
| Newman | |
| USA300_FPR3757 |
⊟Alignments[edit | edit source]
- alignment of orthologues: CLUSTAL format alignment by MAFFT L-INS-i (v7.307)
COL MLNSFDAAYHSLCEEVLEIGNTRNDRTNTGTISKFGHQLRFDLSKGFPLLTTKKVSFKLV
N315 MLNSFDAAYHSLCEEVLEIGNTRNDRTNTGTISKFGHQLRFDLSKGFPLLTTKKVSFKLV
NCTC8325 MLNSFDAAYHSLCEEVLEIGNTRNDRTNTGTISKFGHQLRFDLSKGFPLLTTKKVSFKLV
Newman MLNSFDAAYHSLCEEVLEIGNTRNDRTNTGTISKFGHQLRFDLSKGFPLLTTKKVSFKLV
USA300_FPR3757 MLNSFDAAYHSLCEEVLEIGNTRNDRTNTGTISKFGHQLRFDLSKGFPLLTTKKVSFKLV
************************************************************
COL ATELLWFIKGDTNIQYLLKYNNNIWNEWAFENYIKSDEYKGPDMTDFGHRALSDPEFNEQ
N315 ATELLWFIKGDTNIQYLLKYNNNIWNEWAFENYIKSDEYNGPDMTDFGHRALSDPEFNEQ
NCTC8325 ATELLWFIKGDTNIQYLLKYNNNIWNEWAFENYIKSDEYKGPDMTDFGHRALSDPEFNEQ
Newman ATELLWFIKGDTNIQYLLKYNNNIWNEWAFENYIKSDEYKGPDMTDFGHRALSDPEFNEQ
USA300_FPR3757 ATELLWFIKGDTNIQYLLKYNNNIWNEWAFENYIKSDEYKGPDMTDFGHRALSDPEFNEQ
***************************************:********************
COL YKEQMKQFKQRILEDDTFAKQFGDLGNVYGKQWRDWVDKDGNHFDQLKTVIEQIKHNPDS
N315 YKEQMKQFKQRILEDDTFAKQFGDLGNVYGKQWRDWVDKDGNHFDQLKTVIEQIKHNPDS
NCTC8325 YKEQMKQFKQRILEDDTFAKQFGDLGNVYGKQWRDWVDKDGNHFDQLKTVIEQIKHNPDS
Newman YKEQMKQFKQRILEDDTFAKQFGDLGNVYGKQWRDWVDKDGNHFDQLKTVIEQIKHNPDS
USA300_FPR3757 YKEQMKQFKQRILEDDTFAKQFGDLGNVYGKQWRDWVDKDGNHFDQLKTVIEQIKHNPDS
************************************************************
COL RRHIVSAWNPTEIDTMALPPCHTMFQFYVQDGKLSCQLYQRSADIFLGVPFNIASYALLT
N315 RRHIVSAWNPTEIDTMALPPCHTMFQFYVQDGKLSCQLYQRSADIFLGVPFNIASYALLT
NCTC8325 RRHIVSAWNPTEIDTMALPPCHTMFQFYVQDGKLSCQLYQRSADIFLGVPFNIASYALLT
Newman RRHIVSAWNPTEIDTMALPPCHTMFQFYVQDGKLSCQLYQRSADIFLGVPFNIASYALLT
USA300_FPR3757 RRHIVSAWNPTEIDTMALPPCHTMFQFYVQDGKLSCQLYQRSADIFLGVPFNIASYALLT
************************************************************
COL HLIAKECGLEVGEFVHTFGDAHIYSNHIDAIQTQLARESFNPPTLKINSDKSIFDINYED
N315 HLIAKECGLEVGEFVHTFGDAHIYSNHIDAIQTQLARESFNPPTLKINSDKSIFDINYED
NCTC8325 HLIAKECGLEVGEFVHTFGDAHIYSNHIDAIQTQLARESFNPPTLKINSDKSIFDINYED
Newman HLIAKECGLEVGEFVHTFGDAHIYSNHIDAIQTQLARESFNPPTLKINSDKSIFDINYED
USA300_FPR3757 HLIAKECGLEVGEFVHTFGDAHIYSNHIDAIQTQLARESFNPPTLKINSDKSIFDINYED
************************************************************
COL LEIVDYESHPAIKAPIAV
N315 LEIVDYESHPAIKAPIAV
NCTC8325 LEIVDYESHPAIKAPIAV
Newman LEIVDYESHPAIKAPIAV
USA300_FPR3757 LEIVDYESHPAIKAPIAV
******************
- ↑ Indranil Chatterjee, Andre Kriegeskorte, Andreas Fischer, Susanne Deiwick, Nadine Theimann, Richard A Proctor, Georg Peters, Mathias Herrmann, Barbara C Kahl
In vivo mutations of thymidylate synthase (encoded by thyA) are responsible for thymidine dependency in clinical small-colony variants of Staphylococcus aureus.
J Bacteriol: 2008, 190(3);834-42
[PubMed:17905979] [WorldCat.org] [DOI] (I p)Silke Besier, Johannes Zander, Barbara C Kahl, Peter Kraiczy, Volker Brade, Thomas A Wichelhaus
The thymidine-dependent small-colony-variant phenotype is associated with hypermutability and antibiotic resistance in clinical Staphylococcus aureus isolates.
Antimicrob Agents Chemother: 2008, 52(6);2183-9
[PubMed:18378706] [WorldCat.org] [DOI] (I p)Mariko Ikuo, Chikara Kaito, Kazuhisa Sekimizu
The cvfC operon of Staphylococcus aureus contributes to virulence via expression of the thyA gene.
Microb Pathog: 2010, 49(1-2);1-7
[PubMed:20347953] [WorldCat.org] [DOI] (I p)Andre Kriegeskorte, Desiree Block, Mike Drescher, Nadine Windmüller, Alexander Mellmann, Cathrin Baum, Claudia Neumann, Nicola Ivan Lorè, Alessandra Bragonzi, Eva Liebau, Patrick Hertel, Jochen Seggewiss, Karsten Becker, Richard A Proctor, Georg Peters, Barbara C Kahl
Inactivation of thyA in Staphylococcus aureus attenuates virulence and has a strong impact on metabolism and virulence gene expression.
mBio: 2014, 5(4);e01447-14
[PubMed:25073642] [WorldCat.org] [DOI] (I e)