FOLC_BOVIN
ID FOLC_BOVIN Reviewed; 585 AA.
AC A6H751;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Folylpolyglutamate synthase, mitochondrial;
DE EC=6.3.2.17;
DE AltName: Full=Folylpoly-gamma-glutamate synthetase;
DE Short=FPGS;
DE AltName: Full=Tetrahydrofolate synthase;
DE AltName: Full=Tetrahydrofolylpolyglutamate synthase;
DE Flags: Precursor;
GN Name=FPGS;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes conversion of folates to polyglutamate derivatives
CC allowing concentration of folate compounds in the cell and the
CC intracellular retention of these cofactors, which are important
CC substrates for most of the folate-dependent enzymes that are involved
CC in one-carbon transfer reactions involved in purine, pyrimidine and
CC amino acid synthesis. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + ATP + L-
CC glutamate = (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n+1) + ADP +
CC H(+) + phosphate; Xref=Rhea:RHEA:10580, Rhea:RHEA-COMP:14738,
CC Rhea:RHEA-COMP:14740, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:141005,
CC ChEBI:CHEBI:456216; EC=6.3.2.17;
CC -!- COFACTOR:
CC Name=a monovalent cation; Xref=ChEBI:CHEBI:60242;
CC Evidence={ECO:0000250};
CC Note=A monovalent cation. {ECO:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolylpolyglutamate
CC biosynthesis.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q05932}. Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q05932}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q05932}.
CC -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family.
CC {ECO:0000305}.
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DR EMBL; BC146114; AAI46115.1; -; mRNA.
DR RefSeq; NP_001019651.2; NM_001024480.2.
DR AlphaFoldDB; A6H751; -.
DR SMR; A6H751; -.
DR STRING; 9913.ENSBTAP00000032691; -.
DR PaxDb; A6H751; -.
DR GeneID; 505809; -.
DR KEGG; bta:505809; -.
DR CTD; 2356; -.
DR eggNOG; KOG2525; Eukaryota.
DR InParanoid; A6H751; -.
DR UniPathway; UPA00850; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IBA:GO_Central.
DR GO; GO:0009396; P:folic acid-containing compound biosynthetic process; IBA:GO_Central.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046901; P:tetrahydrofolylpolyglutamate biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.1190.10; -; 1.
DR Gene3D; 3.90.190.20; -; 1.
DR InterPro; IPR001645; Folylpolyglutamate_synth.
DR InterPro; IPR018109; Folylpolyglutamate_synth_CS.
DR InterPro; IPR023600; Folylpolyglutamate_synth_euk.
DR InterPro; IPR036565; Mur-like_cat_sf.
DR InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR InterPro; IPR013221; Mur_ligase_cen.
DR PANTHER; PTHR11136; PTHR11136; 1.
DR PANTHER; PTHR11136:SF5; PTHR11136:SF5; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR PIRSF; PIRSF038895; FPGS; 1.
DR SUPFAM; SSF53244; SSF53244; 1.
DR SUPFAM; SSF53623; SSF53623; 1.
DR TIGRFAMs; TIGR01499; folC; 1.
DR PROSITE; PS01011; FOLYLPOLYGLU_SYNT_1; 1.
DR PROSITE; PS01012; FOLYLPOLYGLU_SYNT_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Ligase; Magnesium; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding;
KW One-carbon metabolism; Phosphoprotein; Reference proteome; Transit peptide.
FT TRANSIT 1..39
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 40..585
FT /note="Folylpolyglutamate synthase, mitochondrial"
FT /id="PRO_0000339186"
FT REGION 477..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 103..106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P08192"
FT BINDING 127
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08192"
FT BINDING 198
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08192"
FT BINDING 226
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08192"
FT BINDING 361
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P08192"
FT BINDING 375
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P08192"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05932"
SQ SEQUENCE 585 AA; 64900 MW; 9F71D76D0754C466 CRC64;
MSRARCHALF LAAVSPRGAT TRVAVRRGLS AWPVLQEPDM EYQDAVRTLN TLQTNANYLE
MVKRKRGDPQ TQLEAMKLYL ARSGLQVEDL DQLNIIHITG TKGKGSTCAF TERILRSYGL
KTGFFSSPHL VQVRERIRIN GQPISSELFT KHFWRLYHRL EETKDDSSCV SMPGYFRFLT
LMAFHVFLQE KVDLAVLEVG IGGAYDCTNI IRKPVVCGIT SLGIDHTGLL GDTMEKIAWQ
KGGIFKSGVP AFTVLQPDEP LAVLRDRAQQ ISCPLYLCPP LQALEEGGPP LTLGLEGEHQ
RSNAALALQV ARCWLQQKGY QDAGELKASR PSLPGQLPLA PVFQPTPRMQ QGLRHTEWPG
RTQLLRRGPL TWYLDGAHTT SSMQACVRWF RQALHRCERP DSGSEVRVLL FNSTGDRDSA
ALLKLLQPCQ FDYAIFCPNL AEMASTDNAD QQNFTVTLDQ VLLRCLAHQQ HWSRLHEEQV
SPDPWSTPGQ EQDGPASLLL APHPPHTHSA SSLVFSCISH ALQWITQGRD PLFQPPSPPR
GLLAHPVADS GATVLQEAAD IHVLVTGSLH LVGGVLKLLE PSLSQ
