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
//