ID A0A136J1F6_9PEZI Unreviewed; 940 AA.
AC A0A136J1F6;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Formate-tetrahydrofolate ligase {ECO:0000313|EMBL:KXJ90904.1};
GN ORFNames=Micbo1qcDRAFT_135219 {ECO:0000313|EMBL:KXJ90904.1};
OS Microdochium bolleyi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Microdochiaceae; Microdochium.
OX NCBI_TaxID=196109 {ECO:0000313|EMBL:KXJ90904.1, ECO:0000313|Proteomes:UP000070501};
RN [1] {ECO:0000313|Proteomes:UP000070501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J235TASD1 {ECO:0000313|Proteomes:UP000070501};
RG DOE Joint Genome Institute;
RA David A.S., May G., Haridas S., Lim J., Wang M., Labutti K., Lipzen A.,
RA Barry K., Grigoriev I.V.;
RT "Draft genome sequence of Microdochium bolleyi, a fungal endophyte of
RT beachgrass.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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; KQ964251; KXJ90904.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136J1F6; -.
DR STRING; 196109.A0A136J1F6; -.
DR InParanoid; A0A136J1F6; -.
DR OrthoDB; 651667at2759; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000070501; Unassembled WGS sequence.
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: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; PS00722; FTHFS_2; 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:KXJ90904.1};
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:UP000070501}.
FT DOMAIN 6..122
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00763"
FT DOMAIN 127..289
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF02882"
SQ SEQUENCE 940 AA; 100471 MW; FF1C6A0038B6834F CRC64;
MAATRLDGTA IAKSIRERLA KDIAAKQQSN PRFQPSLKII QVGDRPDSST YVRMKLKAAQ
EANIHCELMH YPESIPEAEL LAHLHVLNND ASVFGVLVQL PLPSHIDEYA VTSAVADEKD
VDGFGTRNIG ELAKKGGSPY FVPCTPKGVM VLLKEAGVDP KGKNAVVLGR SDIVGSPVSY
LLKNADATVT VCHSKTDNIA EKVKQADIVV AAIGQAGFVK GEWLKPGAVV IDVGTNFIDD
ATKKSGKRLV GDVDFESASE VASVITPVPG GVGPMTVAML LQNVVDSTTA YFDRQKQRAI
VPLPLALKSP VPSDIDVSRS QVPKQITRVA KEVGIAPHEL EQHGAYKAKV DLSLLKRLEH
RRNGRYVVVT GITPTPLGEG KSTTTMGLAQ ALGAHLGRIT FANVRQPSQG PTFGIKGGAA
GGGYSQVIPM DEFNLHLTGD IHAVTAANNL LAAAIETRIF HENTQKDAAL YKRLVPAKNG
TRTFAPIFFR RLKKLGIDKT NPDDLTEEEI RRFARLDIDP ETITWRRVLD VNDRHLRGIN
VGIAPTEKGQ TRETGFDISV ASECMAILAM STDLADMRER LGRMVVATSR SGDPVTCDDV
GAGGALTALM KDAIKPNLMQ TLEGTPVFVH AGPFANISIG NSSILADKMA LKLVGTEPDE
DHAAKAGFAV TEAGFDFTMG GERFFNIKCR ASGLVPDVVV IVATVRALKV HGGGPPITPG
APLHAVYKEE NVEILRKGCV NLKKHIENAK SYGCPVVVAV NKFATDTDAE IAALREEAIA
AGAEDAIMAN HWAEGGKGAI DLAKGVIAAS EKPKDFKLLY ETEGGSVQER METICKKMYG
AAAVEFSELA QKKVDTYTRQ GFANLPICVA KTQYSLSHDP ELKGAPTGFT VPVRDVRMAA
GAGYLYALAA DIQTIPGLPT APGYLNVDVD VETGEVQGLF
//