ID   SUGFT_MYCTO             Reviewed;         234 AA.
AC   P9WKZ2; L0TFA5; P65073; Q50721;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=dTDP-4-amino-4,6-dideoxyglucose formyltransferase {ECO:0000250|UniProtKB:P9WKZ3};
DE            Short=dTDP-Qui4N formyltransferase {ECO:0000250|UniProtKB:P9WKZ3};
DE            EC=2.1.2.- {ECO:0000250|UniProtKB:P9WKZ3};
DE   AltName: Full=Sugar N-formyltransferase MT3512 {ECO:0000305};
GN   OrderedLocusNames=MT3512;
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: Sugar N-formyltransferase that catalyzes the conversion of
CC       dTDP-4-amino-4,6-dideoxyglucose into dTDP-4-formamido-4,6-
CC       dideoxyglucose using N(10)-formyltetrahydrofolate as the carbon source.
CC       Plays a role in virulence. {ECO:0000250|UniProtKB:P9WKZ3}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-10-formyltetrahydrofolate + dTDP-4-amino-4,6-dideoxy-
CC         alpha-D-glucose = (6S)-5,6,7,8-tetrahydrofolate + dTDP-4-formamido-
CC         4,6-dideoxy-alpha-D-glucose + H(+); Xref=Rhea:RHEA:54032,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57453, ChEBI:CHEBI:57454,
CC         ChEBI:CHEBI:68501, ChEBI:CHEBI:138034;
CC         Evidence={ECO:0000250|UniProtKB:P9WKZ3};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WKZ3}.
CC   -!- SIMILARITY: Belongs to the dTDP-Qui4N formyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK47850.1; -; Genomic_DNA.
DR   PIR; A70736; A70736.
DR   RefSeq; WP_003417980.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WKZ2; -.
DR   SMR; P9WKZ2; -.
DR   EnsemblBacteria; AAK47850; AAK47850; MT3512.
DR   GeneID; 45427400; -.
DR   KEGG; mtc:MT3512; -.
DR   PATRIC; fig|83331.31.peg.3770; -.
DR   HOGENOM; CLU_096083_0_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0016742; F:hydroxymethyl-, formyl- and related transferase activity; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR002376; Formyl_transf_N.
DR   InterPro; IPR036477; Formyl_transf_N_sf.
DR   InterPro; IPR040660; N_formyltrans_C.
DR   Pfam; PF00551; Formyl_trans_N; 1.
DR   Pfam; PF18216; N_formyltrans_C; 1.
DR   SUPFAM; SSF53328; SSF53328; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Transferase.
FT   CHAIN           1..234
FT                   /note="dTDP-4-amino-4,6-dideoxyglucose formyltransferase"
FT                   /id="PRO_0000427569"
FT   ACT_SITE        81
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKZ3"
FT   BINDING         9
FT                   /ligand="dTDP-4-amino-4,6-dideoxy-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:68501"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKZ3"
FT   BINDING         62..64
FT                   /ligand="dTDP-4-amino-4,6-dideoxy-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:68501"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKZ3"
FT   BINDING         65..67
FT                   /ligand="(6S)-10-formyltetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57454"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKZ3"
FT   BINDING         90..94
FT                   /ligand="dTDP-4-amino-4,6-dideoxy-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:68501"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKZ3"
FT   BINDING         112
FT                   /ligand="(6S)-10-formyltetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57454"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKZ3"
FT   BINDING         116
FT                   /ligand="(6S)-10-formyltetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57454"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKZ3"
FT   BINDING         175
FT                   /ligand="(6S)-10-formyltetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57454"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKZ3"
FT   BINDING         209
FT                   /ligand="dTDP-4-amino-4,6-dideoxy-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:68501"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKZ3"
SQ   SEQUENCE   234 AA;  26515 MW;  63FF857BB6FFAA8F CRC64;
     MTILILTDNV HAHALAVDLQ ARHGDMDVYQ SPIGQLPGVP RCDVAERVAE IVERYDLVLS
     FHCKQRFPAA LIDGVRCVNV HPGFNPYNRG WFPQVFSIID GQKVGVTIHE IDDQLDHGPI
     IAQRECAIES WDSSGSVYAR LMDIERELVL EHFDAIRDGS YTAKSPATEG NLNLKKDFEQ
     LRRLDLNERG TFGHFLNRLR ALTHDDFRNA WFVDASGRKV FVRVVLEPEK PAEA