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Database: UniProt
Entry: A0A0B1ZZR6_9MICO
LinkDB: A0A0B1ZZR6_9MICO
Original site: A0A0B1ZZR6_9MICO 
ID   A0A0B1ZZR6_9MICO        Unreviewed;       290 AA.
AC   A0A0B1ZZR6;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   31-JUL-2019, entry version 24.
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=LK09_20250 {ECO:0000313|EMBL:KHK95057.1};
OS   Microbacterium mangrovi.
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1348253 {ECO:0000313|EMBL:KHK95057.1, ECO:0000313|Proteomes:UP000031030};
RN   [1] {ECO:0000313|EMBL:KHK95057.1, ECO:0000313|Proteomes:UP000031030}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MUSC 115 {ECO:0000313|EMBL:KHK95057.1,
RC   ECO:0000313|Proteomes:UP000031030};
RA   Lee L.-H.;
RT   "Genome sequence of Microbacterium mangrovi MUSC 115(T).";
RL   Submitted (NOV-2014) 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:KHK95057.1}.
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DR   EMBL; JTDK01000029; KHK95057.1; -; Genomic_DNA.
DR   RefSeq; WP_039403759.1; NZ_JTDK01000029.1.
DR   EnsemblBacteria; KHK95057; KHK95057; LK09_20250.
DR   OrthoDB; 979667at2; -.
DR   UniPathway; UPA00074; UER00170.
DR   Proteomes; UP000031030; 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_C; 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.
DR   PROSITE; PS51671; ACT; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000031030};
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:UP000031030}.
FT   DOMAIN       11     93       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   ACT_SITE    235    235       {ECO:0000256|HAMAP-Rule:MF_01927}.
SQ   SEQUENCE   290 AA;  31936 MW;  3A5B944AF685111B CRC64;
     MPANTQSDHA CLIVHGSDKP GIIAALSALI ARNQGNIVTF DQYSDDAEGG AYFCRVVFHR
     PNFAVAVPEI EADLARTLGE EFDLNWSLAD RSVPKRMAIL ASKQDHCLLD LLWRHRRGDL
     PVSIPMVISN HTTSADDVRS FGVPFFHVPS TPGPDKSESE AKLIELLAGN VDFIVLARYM
     QILSPEFLDA VGVPVINIHH SFLPAFIGAE PYKKAKQRGV KLIGATSHYV TGDLDEGPII
     EQDTIRVTHA DSAAELARRG ADVERQVLSR AVLWHAEDRV IRHGNHTIVF
//
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