PURU_MYCTU
ID PURU_MYCTU Reviewed; 310 AA.
AC P9WHM3; 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 39.
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=Rv2964;
GN ORFNames=MTCY349.23c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Smith D.R., Robison K.;
RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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; U00024; AAA50945.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP45768.1; -; Genomic_DNA.
DR PIR; A70671; A70671.
DR RefSeq; NP_217480.1; NC_000962.3.
DR RefSeq; WP_003899559.1; NZ_NVQJ01000015.1.
DR AlphaFoldDB; P9WHM3; -.
DR SMR; P9WHM3; -.
DR STRING; 83332.Rv2964; -.
DR PaxDb; P9WHM3; -.
DR DNASU; 887338; -.
DR GeneID; 45426952; -.
DR GeneID; 887338; -.
DR KEGG; mtu:Rv2964; -.
DR PATRIC; fig|83332.111.peg.3302; -.
DR TubercuList; Rv2964; -.
DR eggNOG; COG0788; Bacteria.
DR OMA; RTIFHLP; -.
DR PhylomeDB; P9WHM3; -.
DR UniPathway; UPA00074; UER00170.
DR Proteomes; UP000001584; 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 1: Evidence at protein level;
KW Hydrolase; One-carbon metabolism; Purine biosynthesis; Reference proteome.
FT CHAIN 1..310
FT /note="Formyltetrahydrofolate deformylase"
FT /id="PRO_0000074964"
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
