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Database: UniProt
Entry: A0A2I2UGT6_FELCA
LinkDB: A0A2I2UGT6_FELCA
Original site: A0A2I2UGT6_FELCA 
ID   A0A2I2UGT6_FELCA        Unreviewed;       473 AA.
AC   A0A2I2UGT6;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 3.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=5-formyltetrahydrofolate cyclo-ligase {ECO:0000256|ARBA:ARBA00038966};
DE            EC=6.3.3.2 {ECO:0000256|ARBA:ARBA00038966};
GN   Name=LOC101093689 {ECO:0000313|Ensembl:ENSFCAP00000031672.3};
OS   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX   NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000031672.3, ECO:0000313|Proteomes:UP000011712};
RN   [1] {ECO:0000313|Ensembl:ENSFCAP00000031672.3, ECO:0000313|Proteomes:UP000011712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000031672.3,
RC   ECO:0000313|Proteomes:UP000011712};
RX   PubMed=17975172; DOI=10.1101/gr.6380007;
RA   Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA   Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA   Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA   Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA   Tesler G., O'Brien S.J.;
RT   "Initial sequence and comparative analysis of the cat genome.";
RL   Genome Res. 17:1675-1689(2007).
RN   [2] {ECO:0000313|Ensembl:ENSFCAP00000031672.3, ECO:0000313|Proteomes:UP000011712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000031672.3,
RC   ECO:0000313|Proteomes:UP000011712};
RA   Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT   "Sequence assembly of the Felis catus genome version 6.2.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSFCAP00000031672.3}
RP   IDENTIFICATION.
RC   STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000031672.3};
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-5-formyl-5,6,7,8-tetrahydrofolate + ATP = (6R)-5,10-
CC         methenyltetrahydrofolate + ADP + phosphate; Xref=Rhea:RHEA:10488,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57455,
CC         ChEBI:CHEBI:57457, ChEBI:CHEBI:456216; EC=6.3.3.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00036539};
CC   -!- SIMILARITY: Belongs to the 5-formyltetrahydrofolate cyclo-ligase
CC       family. {ECO:0000256|ARBA:ARBA00010638}.
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DR   EMBL; AANG04002993; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A2I2UGT6; -.
DR   STRING; 9685.ENSFCAP00000031672; -.
DR   PaxDb; 9685-ENSFCAP00000011321; -.
DR   Ensembl; ENSFCAT00000041405.3; ENSFCAP00000031672.3; ENSFCAG00000012202.5.
DR   GeneTree; ENSGT00390000017791; -.
DR   InParanoid; A0A2I2UGT6; -.
DR   OMA; YPTQGGH; -.
DR   Proteomes; UP000011712; Chromosome B3.
DR   Bgee; ENSFCAG00000012202; Expressed in spleen and 11 other cell types or tissues.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0030272; F:5-formyltetrahydrofolate cyclo-ligase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0009396; P:folic acid-containing compound biosynthetic process; IBA:GO_Central.
DR   GO; GO:0035999; P:tetrahydrofolate interconversion; IBA:GO_Central.
DR   Gene3D; 3.40.50.10420; NagB/RpiA/CoA transferase-like; 1.
DR   InterPro; IPR002698; FTHF_cligase.
DR   InterPro; IPR024185; FTHF_cligase-like_sf.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   NCBIfam; TIGR02727; MTHFS_bact; 1.
DR   PANTHER; PTHR23407:SF1; 5-FORMYLTETRAHYDROFOLATE CYCLO-LIGASE; 1.
DR   PANTHER; PTHR23407; ATPASE INHIBITOR/5-FORMYLTETRAHYDROFOLATE CYCLO-LIGASE; 1.
DR   Pfam; PF01812; 5-FTHF_cyc-lig; 1.
DR   PRINTS; PR01217; PRICHEXTENSN.
DR   SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011712}.
FT   REGION          1..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          261..307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..59
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        83..105
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..163
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   473 AA;  51030 MW;  BCBBD3EEDD6A62BC CRC64;
     MGQGRAGSRG HAATRSRPRR AEEPPPQSRA EPGQQPPSSD PAPEPAASPD PPPPAPGCTD
     PSRGLHRART LPWTASCSEP HPVPRRPRTP PPPPGSPPSP DPPLGRAEPG YWREAGGGLG
     AGSRRPGSGD EHRGGAGPRD GGGDGREQRQ AEPAGRAEAA SAGDERRGAA ASVPPLGPEG
     ARPRGPPAQR AAPLTERPCA SGLAALRRRR PRRARRHGRA YAPAGAIRTL PPLPGACTSP
     PRVPGPPPGR AHVPLTCRQD YPGRAHAPKP GRSRARARFS GGAHDPPTGP LTKRWSRAEE
     GQGGGGWRPA EVIAHSQYQK SKRISIFLSM QDEVETEEII RDIFRQGKTC FVPRYRFQNS
     HMDMLRLTSP DEISLLPRTS WNILQPGEDE VREEALSTGG LDLIFVPGLG FDKHGNRLGR
     GKGYYDSYLT RCLQQRDSKP YTVALAFREQ MCPRVPVDEH DVRVDEVLYE DST
//
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