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Database: UniProt
Entry: A0A1T3P053_9ACTN
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ID   A0A1T3P053_9ACTN        Unreviewed;       302 AA.
AC   A0A1T3P053;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   08-MAY-2019, entry version 10.
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   ORFNames=B4N89_17465 {ECO:0000313|EMBL:OPC82488.1};
OS   Streptomyces scabrisporus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=159449 {ECO:0000313|EMBL:OPC82488.1, ECO:0000313|Proteomes:UP000190037};
RN   [1] {ECO:0000313|EMBL:OPC82488.1, ECO:0000313|Proteomes:UP000190037}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NF3 {ECO:0000313|EMBL:OPC82488.1,
RC   ECO:0000313|Proteomes:UP000190037};
RA   Vazquez M., Ceapa C.D., Rodriguez Luna D., Sanchez Esquivel S.;
RT   "Draft genome sequence of Streptomyces scabrisporus NF3, endophyte
RT   isolated from Amphipterygium adstringens.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the hydrolysis of 10-formyltetrahydrofolate
CC       (formyl-FH4) to formate and tetrahydrofolate (FH4).
CC       {ECO:0000256|HAMAP-Rule:MF_01927}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-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:57454; 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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OPC82488.1}.
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DR   EMBL; MWQN01000001; OPC82488.1; -; Genomic_DNA.
DR   STRING; 1123320.KB889746_gene8014; -.
DR   UniPathway; UPA00074; UER00170.
DR   Proteomes; UP000190037; Unassembled WGS sequence.
DR   GO; GO:0008864; F:formyltetrahydrofolate deformylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016742; F:hydroxymethyl-, formyl- and related transferase activity; IEA:InterPro.
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; cd08648; FMT_core_Formyl-FH4-Hydrolase_; 1.
DR   HAMAP; MF_01927; PurU; 1.
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   PANTHER; PTHR42706; PTHR42706; 1.
DR   Pfam; PF01842; ACT; 1.
DR   Pfam; PF00551; Formyl_trans_N; 1.
DR   PRINTS; PR01575; FFH4HYDRLASE.
DR   SUPFAM; SSF53328; SSF53328; 1.
DR   TIGRFAMs; TIGR00655; PurU; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000190037};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01927};
KW   One-carbon metabolism {ECO:0000256|HAMAP-Rule:MF_01927};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01927};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190037}.
FT   DOMAIN       24     82       ACT. {ECO:0000259|Pfam:PF01842}.
FT   DOMAIN      106    283       Formyl_trans_N. {ECO:0000259|Pfam:
FT                                PF00551}.
FT   ACT_SITE    246    246       {ECO:0000256|HAMAP-Rule:MF_01927}.
SQ   SEQUENCE   302 AA;  33288 MW;  AF4D5F557E568EC0 CRC64;
     MTEQTQQPLD GTDAGDASTG AGQYVLTLSC PDKRGIVHAV ASFLMMTGCN IVDSQQFGDR
     DTGLFFMRVH FTAEPGVELD ALRAGFTAVG ASFHMDWQIH DGDARMRVFV MVSKFGHCLN
     DLLFRSSIGA LPIEIVGVVS NHRDFEELSR SYGVPFHHIP VTRETKPEAE ARLLALVHEH
     DVELVVLARY MQVLSNDLCK QLEGRAINIH HSFLPSFKGA KPYHQAHARG VKLIGATAHY
     VTGDLDEGPI IEQEVERVDH AVTPAGLVAV GRDVECQALA RAVKWHSERR VLLNGTRTVV
     FT
//
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