ID A0A3B1KIF9_ASTMX Unreviewed; 978 AA.
AC A0A3B1KIF9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=formate--tetrahydrofolate ligase {ECO:0000256|ARBA:ARBA00012295};
DE EC=6.3.4.3 {ECO:0000256|ARBA:ARBA00012295};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000054348.1, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000054348.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 AlphaFoldDB; A0A3B1KIF9; -.
DR STRING; 7994.ENSAMXP00000054348; -.
DR Ensembl; ENSAMXT00000052983.1; ENSAMXP00000054348.1; ENSAMXG00000030844.1.
DR GeneTree; ENSGT00940000157477; -.
DR InParanoid; A0A3B1KIF9; -.
DR OrthoDB; 651667at2759; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000030844; Expressed in embryo and 14 other cell types or tissues.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004329; F:formate-tetrahydrofolate ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; IEA:InterPro.
DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR CDD; cd00477; FTHFS; 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 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; IPR020631; THF_DH/CycHdrlase_NAD-bd_dom.
DR PANTHER; PTHR48099; C-1-TETRAHYDROFOLATE SYNTHASE, CYTOPLASMIC-RELATED; 1.
DR PANTHER; PTHR48099:SF12; MONOFUNCTIONAL C1-TETRAHYDROFOLATE SYNTHASE, MITOCHONDRIAL; 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.
PE 3: Inferred from homology;
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW Reference proteome {ECO:0000313|Proteomes:UP000018467}.
FT DOMAIN 77..183
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00763"
FT DOMAIN 187..333
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF02882"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 978 AA; 105471 MW; 0A2B3BA678126601 CRC64;
MRLSAALRHA CRTSRSGAGQ VRVLSPRGSS TAREERSAGW APVRGTHYTS GSSGGSSAHS
LSLQSRSPRL RAEHQHAARE IIEKSREELA SVLKAHPAIK PTLAIIQAGE DDILLEMNTM
MAEKVGLNVM QICLPRHCTE EEVIEEVLRL NEDQNVHGVF LCLPPSILSR RILNTIKPEK
DVDGVSDLNV GRLVSGALSE GFPSPVAGAV LELLSRQDAS LAGKRAVLVG LEGPLKVILQ
YLLQDAGMEV QTSRWAADNL QKQVKQVDVV VVMGTENTDL LPISVKPGVT VINCGSALMP
EISAAEERAR EAECWTEIGP ISAALRMQNV VRSSVRWVEN QQYQTWTLRP LKLQPLSPVP
SDIEISRAQT PKPIVQLAEE IGLLPEELEA YGRTKAKVRL SLLTRLQNQP NGKYVLVAGI
TPTPLGEGKS TVTIGLVQAL SAHLKLNSFA CLRQPSQGPT FGVKGGAAGG GYAQVIPMEE
FNLHLTGDIH AITAANNLVA AAVDARILHE ATQSDKALYN RLVPSVNGVR RFSPIQLGRL
QRLGINKSDP GTLTPEEVRS FVRLDLDPAK VTWQRVVDTN DRFLRKITVG QANTEKGHSR
QTQFDIAVAS EIMAILALTD GLADMKSRLG RMVVGSSRSG QPVTADDLGV TGALAVLMKD
AIKPTLMQTL EGTPVFVHAG PFANIAHGNS SVLADQLALK LVGEDGFVVT EAGFGADIGM
EKFFNIKCRA SGLKPDVVVL VATIRALKMH GGGPSVTAGA PLPKEYIDEN LQLVSEGCSN
LKKQIEIARL FGVPVVVALN VFKTDTEAEV DLVCRIAEAS GASAAVPCHH WTRGGRGSVE
LARAVKETAA QENDFHFLYS LQTPIVEKIR TIAQKVYGAD DIELSPEAQA KIEYYNQQGF
DTLPVCMAKT HLSLSHMPDK KGVPTGFILP IRDVRASIGA GFIYPLVGTM STMPGLPTRP
CFYDIDLDPN TEEITGLF
//
