SUGFT_MYCBO
ID SUGFT_MYCBO Reviewed; 234 AA.
AC P65074; A0A1R3Y4T5; Q50721; X2BNC5;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 88.
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 BQ2027_MB3438C {ECO:0000305};
GN OrderedLocusNames=BQ2027_MB3438C;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
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; LT708304; SIU02066.1; -; Genomic_DNA.
DR RefSeq; NP_857078.1; NC_002945.3.
DR RefSeq; WP_003417980.1; NC_002945.4.
DR AlphaFoldDB; P65074; -.
DR SMR; P65074; -.
DR EnsemblBacteria; SIU02066; SIU02066; BQ2027_MB3438C.
DR GeneID; 45427400; -.
DR PATRIC; fig|233413.5.peg.3773; -.
DR OMA; TIHEMDE; -.
DR Proteomes; UP000001419; 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_0000014152"
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
