ID A0A094E636_9PEZI Unreviewed; 1179 AA.
AC A0A094E636;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=tetrahydrofolate synthase {ECO:0000256|ARBA:ARBA00013025};
DE EC=6.3.2.17 {ECO:0000256|ARBA:ARBA00013025};
DE AltName: Full=Folylpoly-gamma-glutamate synthetase {ECO:0000256|ARBA:ARBA00030876};
DE AltName: Full=Tetrahydrofolylpolyglutamate synthase {ECO:0000256|ARBA:ARBA00030592};
GN ORFNames=V499_07885 {ECO:0000313|EMBL:KFY71913.1};
OS Pseudogymnoascus sp. VKM F-103.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420912 {ECO:0000313|EMBL:KFY71913.1, ECO:0000313|Proteomes:UP000029295};
RN [1] {ECO:0000313|EMBL:KFY71913.1, ECO:0000313|Proteomes:UP000029295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-103 {ECO:0000313|EMBL:KFY71913.1,
RC ECO:0000313|Proteomes:UP000029295};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00029332};
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolylpolyglutamate
CC biosynthesis. {ECO:0000256|ARBA:ARBA00005150}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family.
CC {ECO:0000256|ARBA:ARBA00008276}.
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:KFY71913.1}.
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DR EMBL; JPKB01001260; KFY71913.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094E636; -.
DR HOGENOM; CLU_273210_0_0_1; -.
DR UniPathway; UPA00850; -.
DR Proteomes; UP000029295; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:InterPro.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR InterPro; IPR001645; Folylpolyglutamate_synth.
DR InterPro; IPR017981; GPCR_2-like_7TM.
DR InterPro; IPR036565; Mur-like_cat_sf.
DR InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR NCBIfam; TIGR01499; folC; 1.
DR PANTHER; PTHR11136:SF5; FOLYLPOLYGLUTAMATE SYNTHASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11136; FOLYLPOLYGLUTAMATE SYNTHASE-RELATED; 1.
DR Pfam; PF05462; Dicty_CAR; 1.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 86..107
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 119..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 167..188
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 304..323
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 8..197
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 236..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..446
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..559
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1179 AA; 130144 MW; DDD06563B5F58432 CRC64;
MSLSARQLRA IEITERTCSI ISLLSSSFVI ITFISSRRFR KPINRLIFYA SWGNCFANVA
TVISVTGVSH GVDGPLCQFQ GFLLQWFILA DAIWAFCMAF NVYLTLFRKY DVTELRKLEW
KYCIASYGVP FIPSFVYLFI KTKARGKIYG SAIQWCWVRT EWGFLRIAMV FAPAWALIVL
SATIYIFAGR KILHSRRRLK SLAKGSLGSS SMAQNEIGFP RATDLEIADE GHLALENGAS
SSNPHGDLGL EMTSNHRPEY PSDPVHTGSE TVMSSSNRPL GDTQSRANPA AKDRRASFDA
NSIIWTYSKF SILFLLALLV TWIPPTSNRI YNFVNSAPNF TLAYLTADEM GSGCDRRTVA
TATQTTMLTT PRIAVIRITG KGSRRSGVVR KVRLARRGQV LARRLGRRGR RVVVETKRRA
EDKAQWQEKR RTKGGKAWIG ARDEEGDGGD GGEESSDLFM YSTVRGEKET ERRRRREGDG
EKETERRRRR EGDGEKETER RRRREGDGEK ETERRRRREG DGEKETERRR RREGDGEKET
ERRRRREGDG GKETERRRYG GFAVSPIDAR GVLSFCAHPP LMCAKPEAEE PEQSSTAFRI
LGFGAYLSST DMICAKPEQH GPGPALTQNK PARPDRLPYS GGSIASLSGP RTTTADAIAL
LDTRRRVRRP SGALAKDAAR DAGLKPEFRV GGEVLRGKPG IVGMSGWMEE LGHSPADVAA
LNIIHVAGTK GKGSTCAYIE ALLLAHGAAT GWPQSVGMYT SPHLLVPQER VRISGTAIDE
RGFAKYFFEV WERLFDGDTA TESQKGERPR YLQLCVLVAL HAFIKEGVGA VVLETHHGGE
YDATNFVEKP VVTVVTPLGR DHVKQLGPGM KDIAWHKAGI LKSGAVAISS AQEEGLEEVL
RARAEERGVF GGDVKVVTGT EEPGVQGVKP DVQMGNCAVA VVAVRAFLER MRGEVLSEES
VRSGVEGFKW PGRFQVVERG GGRERWWCDG AHNEMSIGVA GRWFVDGLEE GDRARVLVFS
QISDSRDTEA VFRCLAESLK GSGVQLVIFT TYDPDQTFSA SMSLDQQVAT TTLPSLDVYE
RVWKELHPNA EVRFEPQLAE ALNLAKLIGE PGAGVDVLVT GSLHLVAGTL WWLGEGVGGI
GSDDAWNLVG TKSLSIGKTE NVMGDVGFGS QEAYGSLDK
//
