ID A3LZQ8_PICST Unreviewed; 995 AA.
AC A3LZQ8;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 2.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=Mitochondrial C1-tetrahydrofolate synthase {ECO:0000313|EMBL:ABN68584.2};
DE EC=6.3.4.3 {ECO:0000313|EMBL:ABN68584.2};
GN Name=MIS1 {ECO:0000313|EMBL:ABN68584.2};
GN ORFNames=PICST_80013 {ECO:0000313|EMBL:ABN68584.2};
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104 {ECO:0000313|EMBL:ABN68584.2, ECO:0000313|Proteomes:UP000002258};
RN [1] {ECO:0000313|EMBL:ABN68584.2, ECO:0000313|Proteomes:UP000002258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC {ECO:0000313|Proteomes:UP000002258};
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
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; CP000502; ABN68584.2; -; Genomic_DNA.
DR RefSeq; XP_001386613.2; XM_001386576.1.
DR AlphaFoldDB; A3LZQ8; -.
DR STRING; 322104.A3LZQ8; -.
DR GeneID; 4840824; -.
DR KEGG; pic:PICST_80013; -.
DR eggNOG; KOG4230; Eukaryota.
DR HOGENOM; CLU_003601_2_0_1; -.
DR InParanoid; A3LZQ8; -.
DR OMA; IKRVVDC; -.
DR OrthoDB; 2047518at2759; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000002258; Chromosome 8.
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; 3.30.1510.10; Domain 2, N(10)-formyltetrahydrofolate synthetase; 2.
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:SF5; 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; PS00766; THF_DHG_CYH_1; 1.
DR PROSITE; PS00767; THF_DHG_CYH_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Ligase {ECO:0000313|EMBL:ABN68584.2};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000002258}.
FT DOMAIN 36..166
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00763"
FT DOMAIN 170..333
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF02882"
SQ SEQUENCE 995 AA; 107095 MW; 394FB77B5E3A4D92 CRC64;
MLSKHISKQL IKPVRVSRLS ARTFSLSSRN LDAVVLSGTK LAKTIRNNIA EKVIHYNQAH
YDEFANIDTI DFTALKFRPN LTIIQVGSRP DSSAYVRSKL KAAQSSNIQS TLVKLDEDIS
QEDLLEEIDR LNKNPKVNGL LIQLPLPKHI DETLVTNSVA TEKDVDGFDR YNVGELSKRG
GSPLFLPCTP SGIIELIKTT GVTLRGKNAV VIGRSDIVGT PVAALLKNED CTVTTCHRYT
KDLPEVVSRA DIVVAAVGIP EYVKAEWIKS DAIVIDVGIN YKEDSTAKNG QKLVGDVDYQ
SVAKKAGFIT PVPGGVGPMT VAMLCSNVFD AAVLQAKKAH EHAFQPLPLQ LKTPVPSDIA
ISRAQKPKKI TKIAQELGIL EKELEPYGHF KAKVDPRSVV ERLDEQVEGS TNEKGHYVLV
AGITPTPLGE GKSTTTMGLT QALGAHLGYN SIANVRQPSM GPTFGVKGGA AGGGYSQVIP
MDEFNMHLTG DIHAISAAQN LLCAAVDTRM FHEATSKTIK GFYKRLVPAK KGERKFTPSM
LKRLQSLGIT KTNPDELTDS EIEKFAHLNI DPASITIKRV VDCNDRFVRE ITIGEGKNEA
SKFPPRKSGM DITVASELMA ILALSTSLKD LRQRVGKVVV GTQKETGIAI TAEDIGCAGA
ITALLKDAIK PNLMQTLEGT PVFVHAGPFA NISIGASSVI ADQLALKLTS PSNPINNGNK
GFVVTEAGFD FTMGGERFFN IKCRASGFKP DTVVLVATSR ALKLHGGAPD VKPGQPLPTE
YVTENIDYLV KGCANLAKQI SNIKQYNVPV VVAINKFETD TDAEIAVIQE QAVKAGAEFA
VPSNHWAEGG AGALDLAKSV VEAVKLSDKS AKQTYLYDVN STVEEKILTI ASKMYGASAI
ELSPLAKQQI ATYTQQGYDK MPICIAKTQY SLSHDPALKG VPTGFTVPIR EVRCSAGAGY
LYALAAEIMT IPGLPTHAGF MNVEVNDDGE IEGLF
//
