ID   PURU_MYCTO              Reviewed;         310 AA.
AC   P9WHM2; L0TDX0; P0A5T6; Q50453;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 40.
DE   RecName: Full=Formyltetrahydrofolate deformylase {ECO:0000255|HAMAP-Rule:MF_01927};
DE            EC=3.5.1.10 {ECO:0000255|HAMAP-Rule:MF_01927};
DE   AltName: Full=Formyl-FH(4) hydrolase {ECO:0000255|HAMAP-Rule:MF_01927};
GN   Name=purU {ECO:0000255|HAMAP-Rule:MF_01927}; OrderedLocusNames=MT3041;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Catalyzes the hydrolysis of 10-formyltetrahydrofolate
CC       (formyl-FH4) to formate and tetrahydrofolate (FH4). {ECO:0000255|HAMAP-
CC       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:0000255|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:0000255|HAMAP-Rule:MF_01927}.
CC   -!- SIMILARITY: Belongs to the PurU family. {ECO:0000255|HAMAP-
CC       Rule:MF_01927}.
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DR   EMBL; AE000516; AAK47366.1; -; Genomic_DNA.
DR   PIR; A70671; A70671.
DR   RefSeq; WP_003899559.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WHM2; -.
DR   SMR; P9WHM2; -.
DR   EnsemblBacteria; AAK47366; AAK47366; MT3041.
DR   GeneID; 45426952; -.
DR   KEGG; mtc:MT3041; -.
DR   PATRIC; fig|83331.31.peg.3281; -.
DR   HOGENOM; CLU_038395_3_0_11; -.
DR   UniPathway; UPA00074; UER00170.
DR   Proteomes; UP000001020; Chromosome.
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; cd04875; ACT_F4HF-DF; 1.
DR   CDD; cd08648; FMT_core_Formyl-FH4-Hydrolase_C; 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   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   SUPFAM; SSF55021; SSF55021; 1.
DR   TIGRFAMs; TIGR00655; PurU; 1.
DR   PROSITE; PS51671; ACT; 1.
PE   3: Inferred from homology;
KW   Hydrolase; One-carbon metabolism; Purine biosynthesis.
FT   CHAIN           1..310
FT                   /note="Formyltetrahydrofolate deformylase"
FT                   /id="PRO_0000428160"
FT   DOMAIN          32..108
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01927"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..28
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        255
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01927"
SQ   SEQUENCE   310 AA;  34006 MW;  2DA6CF44A894BF0A CRC64;
     MGKGSMTAHA TPNEPDYPPP PGGPPPPADI GRLLLRCHDR PGIIAAVSTF LARAGANIIS
     LDQHSTAPEG GTFLQRAIFH LPGLTAAVDE LQRDFGSTVA DKFGIDYRFA EAAKPKRVAI
     MASTEDHCLL DLLWRNRRGE LEMSVVMVIA NHPDLAAHVR PFGVPFIHIP ATRDTRTEAE
     QRQLQLLSGN VDLVVLARYM QILSPGFLEA IGCPLINIHH SFLPAFTGAA PYQRARERGV
     KLIGATAHYV TEVLDEGPII EQDVVRVDHT HTVDDLVRVG ADVERAVLSR AVLWHCQDRV
     IVHHNQTIVF