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Database: UniProt
Entry: W9H0B2_9PROT
LinkDB: W9H0B2_9PROT
Original site: W9H0B2_9PROT 
ID   W9H0B2_9PROT            Unreviewed;       284 AA.
AC   W9H0B2;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   31-JUL-2019, entry version 27.
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   ECO:0000313|EMBL:EWY38127.1};
GN   ORFNames=N825_14495 {ECO:0000313|EMBL:EWY38127.1};
OS   Skermanella stibiiresistens SB22.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Skermanella.
OX   NCBI_TaxID=1385369 {ECO:0000313|EMBL:EWY38127.1, ECO:0000313|Proteomes:UP000019486};
RN   [1] {ECO:0000313|EMBL:EWY38127.1, ECO:0000313|Proteomes:UP000019486}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB22 {ECO:0000313|EMBL:EWY38127.1,
RC   ECO:0000313|Proteomes:UP000019486};
RA   Zhu W., Wang G.;
RT   "The genome sequence of Skermanella stibiiresistens.";
RL   Submitted (AUG-2013) 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:EWY38127.1}.
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DR   EMBL; AVFL01000020; EWY38127.1; -; Genomic_DNA.
DR   RefSeq; WP_037457605.1; NZ_AVFL01000020.1.
DR   EnsemblBacteria; EWY38127; EWY38127; N825_14495.
DR   PATRIC; fig|1385369.3.peg.4773; -.
DR   OrthoDB; 979667at2; -.
DR   UniPathway; UPA00074; UER00170.
DR   Proteomes; UP000019486; 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:UP000019486};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01927,
KW   ECO:0000313|EMBL:EWY38127.1};
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:UP000019486}.
FT   DOMAIN        6     89       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   ACT_SITE    228    228       {ECO:0000256|HAMAP-Rule:MF_01927}.
SQ   SEQUENCE   284 AA;  31814 MW;  BBE9D4D7245B9B4D CRC64;
     MTARYILTIS CPDTVGIVAA VSGFLAERGC NIIDSAQFGD RTSGLFFLRI FLAAPDGGPD
     HAGLAAEFGA IAKRFGMTWH LHDAERRQRL LILVSKFGHC LNDLLYRYRV GGLNVEIPAI
     VSNHRDFYQL AAWHNVPFHY LPVKPDNKAE QEARLWEIVE QERIDLVVLA RYMQVLSPEL
     CDRLAGRAIN IHHSFLPSFK GAKPYHQAFA RGVKLIGATA HYVTSNLDEG PIIEQVVERV
     DHTLTPDDLV EVGRDVESVV LARAVKYHTE HRVLLNGAKT VVFR
//
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