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Database: UniProt/TrEMBL
Entry: Q31PI1_SYNE7
LinkDB: Q31PI1_SYNE7
Original site: Q31PI1_SYNE7 
ID   Q31PI1_SYNE7            Unreviewed;       284 AA.
AC   Q31PI1;
DT   06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT   06-DEC-2005, sequence version 1.
DT   24-JAN-2024, entry version 98.
DE   RecName: Full=Formyltetrahydrofolate deformylase {ECO:0000256|HAMAP-Rule:MF_01927};
DE            EC=3.5.1.10 {ECO:0000256|HAMAP-Rule:MF_01927};
DE   AltName: Full=Formyl-FH(4) hydrolase {ECO:0000256|HAMAP-Rule:MF_01927};
GN   Name=purU {ECO:0000256|HAMAP-Rule:MF_01927};
GN   OrderedLocusNames=Synpcc7942_1008 {ECO:0000313|EMBL:ABB57038.1};
OS   Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805)
OS   (Anacystis nidulans R2).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=1140 {ECO:0000313|EMBL:ABB57038.1, ECO:0000313|Proteomes:UP000889800};
RN   [1] {ECO:0000313|Proteomes:UP000889800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33912 / PCC 7942 / FACHB-805
RC   {ECO:0000313|Proteomes:UP000889800};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the hydrolysis of 10-formyltetrahydrofolate
CC       (formyl-FH4) to formate and tetrahydrofolate (FH4). {ECO:0000256|HAMAP-
CC       Rule:MF_01927}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-10-formyltetrahydrofolate + H2O = (6S)-5,6,7,8-
CC         tetrahydrofolate + formate + H(+); Xref=Rhea:RHEA:19833,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15740,
CC         ChEBI:CHEBI:57453, ChEBI:CHEBI:195366; EC=3.5.1.10;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01927};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       formate from 10-formyl-5,6,7,8-tetrahydrofolate: step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_01927}.
CC   -!- SIMILARITY: Belongs to the PurU family. {ECO:0000256|HAMAP-
CC       Rule:MF_01927}.
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DR   EMBL; CP000100; ABB57038.1; -; Genomic_DNA.
DR   RefSeq; WP_011377827.1; NZ_JACJTX010000003.1.
DR   AlphaFoldDB; Q31PI1; -.
DR   STRING; 1140.Synpcc7942_1008; -.
DR   PaxDb; 1140-Synpcc7942_1008; -.
DR   GeneID; 76399753; -.
DR   KEGG; syf:Synpcc7942_1008; -.
DR   eggNOG; COG0788; Bacteria.
DR   HOGENOM; CLU_038395_3_0_3; -.
DR   OMA; HADHHTD; -.
DR   OrthoDB; 9806170at2; -.
DR   BioCyc; SYNEL:SYNPCC7942_1008-MONOMER; -.
DR   UniPathway; UPA00074; UER00170.
DR   Proteomes; UP000889800; Chromosome.
DR   GO; GO:0008864; F:formyltetrahydrofolate deformylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd04875; ACT_F4HF-DF; 1.
DR   CDD; cd08648; FMT_core_Formyl-FH4-Hydrolase_C; 1.
DR   Gene3D; 3.30.70.260; -; 1.
DR   Gene3D; 3.40.50.170; Formyl transferase, N-terminal domain; 1.
DR   HAMAP; MF_01927; PurU; 1.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR041729; Formyl-FH4-Hydrolase_C.
DR   InterPro; IPR002376; Formyl_transf_N.
DR   InterPro; IPR036477; Formyl_transf_N_sf.
DR   InterPro; IPR004810; PurU.
DR   InterPro; IPR044074; PurU_ACT.
DR   NCBIfam; TIGR00655; PurU; 1.
DR   PANTHER; PTHR42706; FORMYLTETRAHYDROFOLATE DEFORMYLASE; 1.
DR   PANTHER; PTHR42706:SF1; FORMYLTETRAHYDROFOLATE DEFORMYLASE 2, MITOCHONDRIAL; 1.
DR   Pfam; PF00551; Formyl_trans_N; 1.
DR   PIRSF; PIRSF036480; FormyFH4_hydr; 1.
DR   PRINTS; PR01575; FFH4HYDRLASE.
DR   SUPFAM; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF53328; Formyltransferase; 1.
DR   PROSITE; PS51671; ACT; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01927};
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563, ECO:0000256|HAMAP-
KW   Rule:MF_01927}; Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01927};
KW   Reference proteome {ECO:0000313|Proteomes:UP000889800}.
FT   DOMAIN          7..87
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   ACT_SITE        228
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01927"
SQ   SEQUENCE   284 AA;  32201 MW;  AEEF9987DFA9C7B0 CRC64;
     MKRATATLLI SCPDQQGLVA RISNFIFANG GNIIDADQHT DFEAGLFLSR IEWELTGFNL
     DRELIGPAFE AIARPLGAQW QLHFSDRKPR LSLWVSKQDH CLLDLLWRQQ AGELDAEIPL
     IISNHDKLRP IAEQFGIDFL HLPITRETKA EQEARQLAAI ADYGIDLVVL AKYMQVLSSE
     FLAQFPQVIN IHHSFLPAFA GANPYQRAYE RGVKIIGATA HYVTPDLDEG PIIEQDVVRV
     SHRDDADDLV RKGKDLERIV LARAVRLHLQ HRVLTYRNRT VVFA
//
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