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Database: UniProt
Entry: Q6CMZ4_KLULA
LinkDB: Q6CMZ4_KLULA
Original site: Q6CMZ4_KLULA 
ID   Q6CMZ4_KLULA            Unreviewed;       947 AA.
AC   Q6CMZ4;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   27-MAR-2024, entry version 112.
DE   SubName: Full=KLLA0E16545p {ECO:0000313|EMBL:CAG99782.1};
GN   ORFNames=KLLA0_E16545g {ECO:0000313|EMBL:CAG99782.1};
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590 {ECO:0000313|EMBL:CAG99782.1, ECO:0000313|Proteomes:UP000000598};
RN   [1] {ECO:0000313|EMBL:CAG99782.1, ECO:0000313|Proteomes:UP000000598}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
RC   WM37 {ECO:0000313|Proteomes:UP000000598};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA   Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA   Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC       {ECO:0000256|ARBA:ARBA00004777}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the
CC       formate--tetrahydrofolate ligase family.
CC       {ECO:0000256|ARBA:ARBA00006985}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the tetrahydrofolate
CC       dehydrogenase/cyclohydrolase family. {ECO:0000256|ARBA:ARBA00005559}.
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DR   EMBL; CR382125; CAG99782.1; -; Genomic_DNA.
DR   RefSeq; XP_454695.1; XM_454695.1.
DR   AlphaFoldDB; Q6CMZ4; -.
DR   STRING; 284590.Q6CMZ4; -.
DR   PaxDb; 284590-Q6CMZ4; -.
DR   GeneID; 2894215; -.
DR   KEGG; kla:KLLA0_E16545g; -.
DR   eggNOG; KOG4230; Eukaryota.
DR   HOGENOM; CLU_003601_2_0_1; -.
DR   InParanoid; Q6CMZ4; -.
DR   OMA; QPIMFRR; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000000598; Chromosome E.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004329; F:formate-tetrahydrofolate ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004477; F:methenyltetrahydrofolate cyclohydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR   CDD; cd00477; FTHFS; 1.
DR   CDD; cd01080; NAD_bind_m-THF_DH_Cyclohyd; 1.
DR   Gene3D; 3.10.410.10; Formyltetrahydrofolate synthetase, domain 3; 1.
DR   Gene3D; 3.40.50.10860; Leucine Dehydrogenase, chain A, domain 1; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   HAMAP; MF_01543; FTHFS; 1.
DR   HAMAP; MF_01576; THF_DHG_CYH; 1.
DR   InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR   InterPro; IPR000559; Formate_THF_ligase.
DR   InterPro; IPR020628; Formate_THF_ligase_CS.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000672; THF_DH/CycHdrlase.
DR   InterPro; IPR020630; THF_DH/CycHdrlase_cat_dom.
DR   InterPro; IPR020867; THF_DH/CycHdrlase_CS.
DR   InterPro; IPR020631; THF_DH/CycHdrlase_NAD-bd_dom.
DR   PANTHER; PTHR48099:SF8; C-1-TETRAHYDROFOLATE SYNTHASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR48099; C-1-TETRAHYDROFOLATE SYNTHASE, CYTOPLASMIC-RELATED; 1.
DR   Pfam; PF01268; FTHFS; 1.
DR   Pfam; PF00763; THF_DHG_CYH; 1.
DR   Pfam; PF02882; THF_DHG_CYH_C; 1.
DR   PRINTS; PR00085; THFDHDRGNASE.
DR   SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00721; FTHFS_1; 1.
DR   PROSITE; PS00722; FTHFS_2; 1.
DR   PROSITE; PS00767; THF_DHG_CYH_2; 1.
PE   3: Inferred from homology;
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000598}.
FT   DOMAIN          4..120
FT                   /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00763"
FT   DOMAIN          124..291
FT                   /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT                   NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02882"
SQ   SEQUENCE   947 AA;  102381 MW;  C5C7B74C4905C076 CRC64;
     MAIIDGKAIA NGIRDEIKDE ISSLKEKYAV FRPTLTIFQV GNRPDSNTYV KMKLKAAKDA
     GIDVKFIHLD ETVTEVELLG QIDDENSDDS VHGILVQLPL PAHLNEDKIT SRVSACKDVD
     GFGPVNIGEL NKRNGTPYFQ PCTPRGIIEL LKRSGVTIAG SEAVVIGRSD IVGSPVATLL
     TSLDATVTIL HSKSKDLREF ISRADIVVVA IGQPEFIRGE WFANNKRGAV VIDVGTNFVK
     DETRKSGYRN VGDVEFAAAE PYVKLITPVP GGVGPMTVAM LMQNTFESAK RYLDKQLNSG
     NDFEPLKLNL LKPVPSDFEI SRAQVPKPIT QIAAESGILP SELEPYGDTK AKVKLDLLNR
     LKNRENGKYI LVTGITPTPL GEGKSTTTVG LAQALGAHLK KKVFANVRQP SMGPTFGIKG
     GAAGGGYSQV IPMDEFNLHV TGDIHAISMA NNLLAAAIDT RMFHESTQSN AALYKRLVPA
     KKGVRKFTPT MLRRLKKLGI NKTDPNELSA EESARFARLD IDPETITWRR VVDCNDRFLR
     GITVGQAPTE RGHTRYTGFD ISVASECMAV LALANSLEDM RERLGRIVIA ASKSGEPITC
     EDIGCAGAMT ALLKDAIKPN IMQTLEGTPV FVHAGPFANI SIGANSVLAD KMALKLAGVP
     TDLPEDVKKT QKGYVVTEAG FDFTMGGERF INIKCRSSGL VPDVVVIVAT VRALKVHGGG
     PEVKAGAPLP SEYLNEDVEL LRKGCANLAK HISNARAYNL PVVVAINKMS SDTDNEHEVI
     REESIKAGAV DAIVSNHWEE GGKGAVDLAE GIINTANNQS NEDFKFLYEV EGQSVEDKIS
     AIAKEMYGAG EVEFLPEAQA KIDLYTKQGF NNLPICIAKT QYSLSHDANL KGVPTGFKFP
     IRDVRASIGA GYLYALAAEI QTIPGLPTHC GFMNVEVNED GEIDGMF
//
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