ID A0A401RNG9_CHIPU Unreviewed; 875 AA.
AC A0A401RNG9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=C-1-tetrahydrofolate synthase, cytoplasmic {ECO:0000256|ARBA:ARBA00017592};
DE EC=1.5.1.5 {ECO:0000256|ARBA:ARBA00012859};
DE EC=3.5.4.9 {ECO:0000256|ARBA:ARBA00012776};
DE EC=6.3.4.3 {ECO:0000256|ARBA:ARBA00012295};
GN ORFNames=chiPu_0018487 {ECO:0000313|EMBL:GCC19721.1};
OS Chiloscyllium punctatum (Brownbanded bambooshark) (Hemiscyllium punctatum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes; Hemiscylliidae;
OC Chiloscyllium.
OX NCBI_TaxID=137246 {ECO:0000313|EMBL:GCC19721.1, ECO:0000313|Proteomes:UP000287033};
RN [1] {ECO:0000313|EMBL:GCC19721.1, ECO:0000313|Proteomes:UP000287033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-5,10-methenyltetrahydrofolate + H2O = (6R)-10-
CC formyltetrahydrofolate + H(+); Xref=Rhea:RHEA:23700,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57455,
CC ChEBI:CHEBI:195366; EC=3.5.4.9;
CC Evidence={ECO:0000256|ARBA:ARBA00036357};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6R)-10-
CC formyltetrahydrofolate + ADP + phosphate; Xref=Rhea:RHEA:20221,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57453, ChEBI:CHEBI:195366, ChEBI:CHEBI:456216;
CC EC=6.3.4.3; Evidence={ECO:0000256|ARBA:ARBA00036012};
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:GCC19721.1}.
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DR EMBL; BEZZ01001591; GCC19721.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401RNG9; -.
DR STRING; 137246.A0A401RNG9; -.
DR OMA; QPIMFRR; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000287033; 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; 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; 3.
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:SF1; C-1-TETRAHYDROFOLATE SYNTHASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR48099; C-1-TETRAHYDROFOLATE SYNTHASE, CYTOPLASMIC-RELATED; 1.
DR Pfam; PF01268; FTHFS; 3.
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 One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW Reference proteome {ECO:0000313|Proteomes:UP000287033};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..875
FT /note="C-1-tetrahydrofolate synthase, cytoplasmic"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019368902"
FT DOMAIN 44..161
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00763"
FT DOMAIN 165..329
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF02882"
SQ SEQUENCE 875 AA; 94170 MW; 69E7DB8BCC4C76D9 CRC64;
MHGTAHSFSL VARLWGCRLV GMLSHPVNPG KNLGIVRTVA SIVSGVKTSA QVRERLKNEV
VQMKEQAPGF RPGLAILQVG DRDDSNLYIS MKLKAAAEIG MNANHVKLPK TATEDEVLRN
ITHINEDPNV HGLIVQLPLD SINPIDVEKV TNAVAPEKDV DGLTSINAGK LARGDLGDCF
IPCTPNGCLE LIKHTGVKLA GSRAVVIGRS KIVGAPMRDL LVSNHATVTT CHSKTADLPG
EIGRADILVV GAGKAEMVKG NWIKPGAVVI DCGINYIPDS TKPSGKRVVG DVAYNEAKEV
ASYITPVPGG VGPMTVCMLM ANTVEGAKRY LKNCKPGKWP IQYTKLKLVE PVPSDIVISR
SCTPKHISRM AKEVGLLSDE VELYGKSKAK VLLTTINRLK DQPDGKYVVV TGITPTPLGE
GKSTTTIGLA QAIGAHLDIN VFACVRQPSQ GPTFGIKGGA AGGGYSQVIP MEEFNLHLTG
DIHAITAANN LVAAAIDARM FHEATQSDKA LYDRLVPSNK GVRAFSQIQL RRLQKLGINK
TEPTALTEEE IHRFVRLDIE PDTITWQRVM DTNDRFLRKI TIGQSSTEKG YTRTGISGAL
AVLMKDAIKP NLMQTLEGTP VFVHAGPFAN IAHGNSSILA DKIALKLVGP AGFVAGVPLP
KEYIEENLDL LEKGCSNLRK QIENANLFGV SVVVAVNAFK TDTEAELELV CSLAKEMGAF
DAVKCTHWAE GGRGAVELAR AVQRASELDS NFKYLYPLEL PIVDKIQTIA QKIYGAADVE
LSPEAQNKVE LYTKQGFADL PICMAKTHLS LSHMPEKKGA PTGFVLPIRD IRASVGAGFL
YPLVGTMSTM PGLPTRPCFY DIDLDPETEE VNGLF
//
