ID A5DVD5_LODEL Unreviewed; 585 AA.
AC A5DVD5;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Phosphomethylpyrimidine kinase THI20 {ECO:0008006|Google:ProtNLM};
GN ORFNames=LELG_01321 {ECO:0000313|EMBL:EDK43143.1};
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508 {ECO:0000313|EMBL:EDK43143.1, ECO:0000313|Proteomes:UP000001996};
RN [1] {ECO:0000313|EMBL:EDK43143.1, ECO:0000313|Proteomes:UP000001996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 /
RC NRRL YB-4239 {ECO:0000313|Proteomes:UP000001996};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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DR EMBL; CH981524; EDK43143.1; -; Genomic_DNA.
DR RefSeq; XP_001528801.1; XM_001528751.1.
DR AlphaFoldDB; A5DVD5; -.
DR STRING; 379508.A5DVD5; -.
DR GeneID; 5235849; -.
DR KEGG; lel:LELG_01321; -.
DR VEuPathDB; FungiDB:LELG_01321; -.
DR eggNOG; KOG2598; Eukaryota.
DR HOGENOM; CLU_020520_2_1_1; -.
DR InParanoid; A5DVD5; -.
DR OMA; FWEMFPY; -.
DR OrthoDB; 5477821at2759; -.
DR Proteomes; UP000001996; Unassembled WGS sequence.
DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro.
DR CDD; cd01169; HMPP_kinase; 1.
DR CDD; cd19367; TenA_C_ScTHI20-like; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR Gene3D; 1.20.910.10; Heme oxygenase-like; 1.
DR InterPro; IPR016084; Haem_Oase-like_multi-hlx.
DR InterPro; IPR004399; HMP/HMP-P_kinase_dom.
DR InterPro; IPR013749; PM/HMP-P_kinase-1.
DR InterPro; IPR029056; Ribokinase-like.
DR InterPro; IPR004305; Thiaminase-2/PQQC.
DR PANTHER; PTHR20858:SF17; HYDROXYMETHYLPYRIMIDINE_PHOSPHOMETHYLPYRIMIDINE KINASE THI20-RELATED; 1.
DR PANTHER; PTHR20858; PHOSPHOMETHYLPYRIMIDINE KINASE; 1.
DR Pfam; PF08543; Phos_pyr_kin; 1.
DR Pfam; PF03070; TENA_THI-4; 1.
DR SUPFAM; SSF48613; Heme oxygenase-like; 1.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001996}.
FT DOMAIN 28..306
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
FT DOMAIN 342..581
FT /note="Thiaminase-2/PQQC"
FT /evidence="ECO:0000259|Pfam:PF03070"
FT REGION 488..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 585 AA; 65082 MW; C0A0EEF27A538362 CRC64;
MKTNIVSLKL FEEEDVKLPV VLTIAGSDSS GGAGIEADLK TFSAFDVYGM TCITALTAQN
TTGVKTYKET SRELVHEILK ANLEDMYENE EKGPLKVIKT GMLTKSAIEE LAQFDLKIKM
VIDPVMVTTS GSKLLDHEGV KLCVDNLMKN AFLVTPNFVE AETIYKILGK SAQVKQLDEF
IKFTVDLQKM VGCKNILVKG GHIPFDANGK VVEDTTAEGQ AQPQSNPGLK VIDVLYESEN
DVVTIFESKY IESDNSHGTG CTLASAIAAN IAKGTSLADS VAIGIDYIHQ GMLKMSKLGH
GKGPLNHNVK PREAISDLVN TTLNNQVKFD ENFTLLDYLI NHPDVKRNWE TYATHPFVEL
VAKDEMPFEK FFYYLKQDYH YLIVYARMHG LAASKAPTYK ESHAQATIIG EIVTEIEKHK
EKLKAYNVDY DKDDVPPGDA CVRYCNYLLD IGMREDFLGI KVALAPCLHG YADAGAFGKR
ILQQRQHQLK QQEHGSDADA DADTGAGAST NDTVTPHEYL HIYRSWLDDY TSEWFLEADA
AGKEALQRLS ADGLSEHRLK ELVKIFNDVT LLEINFWSEV LELDV
//
