ID G1SIB2_RABIT Unreviewed; 979 AA.
AC G1SIB2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 3.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=formate--tetrahydrofolate ligase {ECO:0000256|ARBA:ARBA00012295};
DE EC=6.3.4.3 {ECO:0000256|ARBA:ARBA00012295};
GN Name=MTHFD1L {ECO:0000313|Ensembl:ENSOCUP00000002415.4};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000002415.4, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000002415.4, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000002415.4,
RC ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000002415.4}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000002415.4};
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 EMBL; AAGW02053513; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02053514; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02053515; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02053516; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02053517; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02053518; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1SIB2; -.
DR SMR; G1SIB2; -.
DR STRING; 9986.ENSOCUP00000002415; -.
DR PaxDb; 9986-ENSOCUP00000002415; -.
DR Ensembl; ENSOCUT00000002783.4; ENSOCUP00000002415.4; ENSOCUG00000002781.4.
DR eggNOG; KOG4230; Eukaryota.
DR GeneTree; ENSGT00940000157477; -.
DR HOGENOM; CLU_003601_0_0_1; -.
DR InParanoid; G1SIB2; -.
DR TreeFam; TF300623; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000001811; Chromosome 12.
DR Bgee; ENSOCUG00000002781; Expressed in uterus and 16 other cell types or tissues.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:Ensembl.
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:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0009257; P:10-formyltetrahydrofolate biosynthetic process; IEA:Ensembl.
DR GO; GO:0048702; P:embryonic neurocranium morphogenesis; IEA:Ensembl.
DR GO; GO:0048703; P:embryonic viscerocranium morphogenesis; IEA:Ensembl.
DR GO; GO:0015942; P:formate metabolic process; IEA:Ensembl.
DR GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
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:UP000001811}.
FT DOMAIN 81..180
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00763"
FT DOMAIN 184..335
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF02882"
FT REGION 30..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 979 AA; 105781 MW; AB27C5452A4C5594 CRC64;
MRARLPLVLR QLGRPLRPPG PPRCLRVPCR AGSGGGGGGG GGRDGLLGHR RLQDGQAWSS
CGPGSPEPPA RDSIVREVIQ NSKEVLSLLQ EKNPAFKPVL AVIQAGDDNL LQEVNQNLAE
EAGLNITHIC LPPDSSEDEI IDEILKMNED ARVHGLSLQV PENSLSSKVL NALKPEKDVD
GVTDVNLGKL VRGDAHECFV SPVARAVIEL LEKSVGVNLD GKKVLVLGAH GPLEAALQCL
FQRKDSMTMS SQWKTPQLES KLQEADIVIL GSPKPEEIPV AWIRPGTTVL NCFHSFMSEK
LGCGSHGVHC GGSIAEDDVS LLAAALRIQN MVSSGRRWLR EQQHRRWRLH CLKLQPLSPV
PSDIEISRGQ TPKAVDVLAK EIGLLAEEIE IYGKSKAKVR LSLLERLKDQ ADGKYVLVAG
ITPTPLGEGK STVTIGLVQA LTAHLNVNSF ACLRQPSQGP TFGVKGGAAG GGYAQVIPME
EFNLHLTGDI HAITAANNLL AAAIDTRILH ENTQTDKALY NRLVPSVNGV REFSEIQLAR
LKKLGINKTD PSALTEEEMG KFARLNIDPS TITWQRVLDT NDRFLRKITI GQASTEKGYS
RQAQFDIAVA SEIMAVLALT DSLADMKERL GRMVVASDKD GQPVTAEDLG VTGALTVLMK
DAIKPNLMQT LEGTPVFVHA GPFANIAHGN SSVLADKIAL KLVGEEGFVV TEAGFGADIG
MEKFFNIKCR ASGLVPNAVV LVATVRALKM HGGGPSVIPG VPLKKEYTEE NIQLVADGCC
NLQKQIQIAQ LFEVPVVVAL NVFKTDTRAE IDLVCELAKR AGAFDAVPCY HWSVGGKGSV
DLARAVREAA NTNSHFQFLY DVQLPIVEKI RKIAQAVYGA KDIELFPEAQ SKIDRYTQQG
FGNLPICMAK THLSLSHQPD KKGVPRDFVL PISDVRASIG AGFIYPLVGT MSTMPGLPTR
PCFYDIDLDT ETEQVQGLF
//
