ID A0A1Y2H4B5_9FUNG Unreviewed; 1071 AA.
AC A0A1Y2H4B5;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Formate--tetrahydrofolate ligase-domain-containing protein {ECO:0000313|EMBL:ORZ27892.1};
GN ORFNames=BCR41DRAFT_346187 {ECO:0000313|EMBL:ORZ27892.1};
OS Lobosporangium transversale.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC Mortierellomycetes; Mortierellales; Mortierellaceae; Lobosporangium.
OX NCBI_TaxID=64571 {ECO:0000313|EMBL:ORZ27892.1, ECO:0000313|Proteomes:UP000193648};
RN [1] {ECO:0000313|EMBL:ORZ27892.1, ECO:0000313|Proteomes:UP000193648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3116 {ECO:0000313|EMBL:ORZ27892.1,
RC ECO:0000313|Proteomes:UP000193648};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ORZ27892.1}.
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DR EMBL; MCFF01000003; ORZ27892.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2H4B5; -.
DR STRING; 64571.A0A1Y2H4B5; -.
DR InParanoid; A0A1Y2H4B5; -.
DR OrthoDB; 651667at2759; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000193648; 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; 1.10.8.770; -; 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; 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:ORZ27892.1};
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:UP000193648}.
FT DOMAIN 139..255
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00763"
FT DOMAIN 258..421
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF02882"
SQ SEQUENCE 1071 AA; 116052 MW; BBCF91BCEA8C7D33 CRC64;
MKVLSTLDRT IHASSHQHSC LHPSFVLTLS SALNLSRRVT PVPAQIRLSH SLFTYCFKSS
PTSRFSSLHH SYPSSSSSHT LSLFSRPIFS TLPRSGPLGY KTLLTLRSLP RHSNFHPYSL
HTSTLALNTR SSFNMAKIID GKAIAQKLRN DIKSQIEEVR KTAPSFSPKL SIIQVGERED
SSVYVNMKKK AAKEAGMDFE LFHLPATITQ YELLSRVQAL NNDPKVHGIL VQLPLPDHLD
DRIVTEAIDP KKDVDGFHAI NIGHLSKRAS EPAFVPCTPK GVIELIKSTD VVMAGKKAVV
VGRSDIVGTP VFSLLTKNNC TVTLCHSKTM NLPEIVKTAD ILVVAIGSAG FIKGEWIKEG
AVVIDVGTNA VEDSTKKAGI RWVGDVEYAT ASQRAGHITP VPGGVGPMTV AMLMQNTYLS
AVRFLNEGRH RTINPLPLQL LDPVPNDIDI ALAQKPKPIK FIADELGILP CELELYGEYK
AKVSLDILER LSHRKNGRYV VVTGITPTPL GEGKSTTTVG LVQALGAHLD KIAFGCVRQP
SQGPTFGIKG GAAGGGYSQV IPMDEFNLHL TGDIHAVTAA NNLLAAAIDA RIFHEKTQSD
KALFSRLCPT KKGKKVFAAV MLGRLQRLGI NKTDPAELTP EEVSRFVRLD IDPETITWQR
VMDTNDRFLR RIEIGRNDTE AGHERMTGFD IAVASEVMAV LALSTDLKDM RERLGKMVVA
SSKAGEPVTA DDIGIGGALT VLMKDAIKPN VMQTLEGTPM FVHAGPFANI AHGNSSIIAD
RIALKLAGIE PGENEEMMGY VVTEAGFGAD IGMEKFFDIK CRTSGLVPDC AVLVATVKAL
KMHGGGPEVT PGKPLPEVYN SENLELLESG CDNLKKHIEN AKKFGVPVVV AINKFTSDTD
AEMALIRKIA LEAGADNAVA CENWAKGGLG AVELGQAVIQ ACSKPINFKY LYSLESDIAS
KIETISKEMY GADGIELSDL AKEKIATYTR QGFGNLPICM AKTHLSLSHD PKLKNRPVGF
KIPIRDIRAS VGAGFLYPLC GAMQTMPGLP TRPCFYDVDI DFETGNVVGL F
//
