WBKC_BRUME
ID WBKC_BRUME Reviewed; 259 AA.
AC F8WJP6; D0B1X4;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=GDP-perosamine N-formyltransferase {ECO:0000305};
DE EC=2.1.2.14 {ECO:0000269|PubMed:28636341};
GN Name=wbkC {ECO:0000303|PubMed:11081580};
GN OrderedLocusNames=BMEI1418 {ECO:0000312|EMBL:AAL52599.1};
GN ORFNames=BAWG_0804 {ECO:0000312|EMBL:EEW88696.1};
OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=224914;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=16M / ATCC 23456 / NCTC 10094;
RX PubMed=11081580; DOI=10.1016/s0923-2508(00)90130-x;
RA Godfroid F., Cloeckaert A., Taminiau B., Danese I., Tibor A., de Bolle X.,
RA Mertens P., Letesson J.J.;
RT "Genetic organisation of the lipopolysaccharide O-antigen biosynthesis
RT region of brucella melitensis 16M (wbk).";
RL Res. Microbiol. 151:655-668(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16M / ATCC 23456 / NCTC 10094;
RX PubMed=11756688; DOI=10.1073/pnas.221575398;
RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA Haselkorn R., Kyrpides N.C., Overbeek R.;
RT "The genome sequence of the facultative intracellular pathogen Brucella
RT melitensis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16M / ATCC 23456 / NCTC 10094;
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L.,
RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T.,
RA White J., Yandava C., Whatmore A.M., Perrett L.L., O'Callaghan D.,
RA Nusbaum C., Galagan J., Birren B.;
RT "The genome sequence of Brucella melitensis bv. 1 str. 16M.";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0007744|PDB:5VYR, ECO:0007744|PDB:5VYS, ECO:0007744|PDB:5VYT, ECO:0007744|PDB:5VYU}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF MUTANTS ALA-78; SER-47/ALA-78 AND
RP ALA-78/ALA-142 IN COMPLEXES WITH GMP; GDP AND TETRAHYDROFOLIC ACID,
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RC STRAIN=16M / ATCC 23456 / NCTC 10094;
RX PubMed=28636341; DOI=10.1021/acs.biochem.7b00494;
RA Riegert A.S., Chantigian D.P., Thoden J.B., Tipton P.A., Holden H.M.;
RT "Biochemical characterization of WbkC, an N-formyltransferase from Brucella
RT melitensis.";
RL Biochemistry 56:3657-3668(2017).
CC -!- FUNCTION: Involved in the lipopolysaccharide (LPS) O-antigen
CC biosynthesis (PubMed:11081580). Catalyzes the transfer of a formyl
CC group to GDP-perosamine, leading to the formation of GDP-N-
CC formylperosamine (PubMed:11081580, PubMed:28636341). In vitro, can also
CC function on GDP-3-deoxyperosamine, thereby providing an enzymatic
CC method for producing a novel trideoxysugar not found in nature
CC (PubMed:28636341). {ECO:0000269|PubMed:11081580,
CC ECO:0000269|PubMed:28636341}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-10-formyltetrahydrofolate + GDP-alpha-D-perosamine =
CC (6S)-5,6,7,8-tetrahydrofolate + GDP-N-formyl-alpha-D-perosamine +
CC H(+); Xref=Rhea:RHEA:68588, ChEBI:CHEBI:15378, ChEBI:CHEBI:57453,
CC ChEBI:CHEBI:57454, ChEBI:CHEBI:73996, ChEBI:CHEBI:176524;
CC EC=2.1.2.14; Evidence={ECO:0000269|PubMed:28636341};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68589;
CC Evidence={ECO:0000269|PubMed:28636341};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis. {ECO:0000269|PubMed:11081580}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:28636341}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant is completely O-antigen-negative.
CC {ECO:0000269|PubMed:11081580}.
CC -!- SIMILARITY: Belongs to the Fmt family. {ECO:0000305}.
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DR EMBL; AE008917; AAL52599.1; -; Genomic_DNA.
DR EMBL; GG703778; EEW88696.1; -; Genomic_DNA.
DR PIR; AD3429; AD3429.
DR RefSeq; WP_002963675.1; NZ_GG703778.1.
DR PDB; 5VYR; X-ray; 1.70 A; A/B=1-259.
DR PDB; 5VYS; X-ray; 2.20 A; A/B=1-259.
DR PDB; 5VYT; X-ray; 2.20 A; A/B/C/D=1-259.
DR PDB; 5VYU; X-ray; 2.20 A; A/B=1-259.
DR PDBsum; 5VYR; -.
DR PDBsum; 5VYS; -.
DR PDBsum; 5VYT; -.
DR PDBsum; 5VYU; -.
DR SMR; F8WJP6; -.
DR STRING; 224914.BMEI1418; -.
DR EnsemblBacteria; AAL52599; AAL52599; BMEI1418.
DR GeneID; 45123991; -.
DR GeneID; 55590265; -.
DR KEGG; bme:BMEI1418; -.
DR KEGG; bmel:DK63_2070; -.
DR PATRIC; fig|224914.52.peg.2170; -.
DR eggNOG; COG0223; Bacteria.
DR OMA; FTHESPY; -.
DR PhylomeDB; F8WJP6; -.
DR UniPathway; UPA00030; -.
DR Proteomes; UP000000419; Chromosome I.
DR Proteomes; UP000008511; Unassembled WGS sequence.
DR GO; GO:0008446; F:GDP-mannose 4,6-dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0016742; F:hydroxymethyl-, formyl- and related transferase activity; IEA:InterPro.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR002376; Formyl_transf_N.
DR InterPro; IPR036477; Formyl_transf_N_sf.
DR Pfam; PF00551; Formyl_trans_N; 1.
DR SUPFAM; SSF53328; SSF53328; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lipopolysaccharide biosynthesis; Transferase.
FT CHAIN 1..259
FT /note="GDP-perosamine N-formyltransferase"
FT /id="PRO_0000455052"
FT BINDING 89..91
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000305|PubMed:28636341"
FT BINDING 139..143
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000305|PubMed:28636341"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:5VYR"
FT HELIX 15..27
FT /evidence="ECO:0007829|PDB:5VYR"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:5VYR"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:5VYR"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:5VYR"
FT HELIX 47..56
FT /evidence="ECO:0007829|PDB:5VYR"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:5VYR"
FT HELIX 68..77
FT /evidence="ECO:0007829|PDB:5VYR"
FT STRAND 80..86
FT /evidence="ECO:0007829|PDB:5VYR"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:5VYR"
FT STRAND 103..110
FT /evidence="ECO:0007829|PDB:5VYR"
FT TURN 111..114
FT /evidence="ECO:0007829|PDB:5VYR"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:5VYR"
FT HELIX 119..125
FT /evidence="ECO:0007829|PDB:5VYR"
FT STRAND 129..136
FT /evidence="ECO:0007829|PDB:5VYR"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:5VYS"
FT STRAND 147..154
FT /evidence="ECO:0007829|PDB:5VYR"
FT HELIX 161..173
FT /evidence="ECO:0007829|PDB:5VYR"
FT HELIX 176..185
FT /evidence="ECO:0007829|PDB:5VYR"
FT HELIX 204..207
FT /evidence="ECO:0007829|PDB:5VYR"
FT HELIX 215..225
FT /evidence="ECO:0007829|PDB:5VYR"
FT STRAND 243..246
FT /evidence="ECO:0007829|PDB:5VYS"
FT HELIX 247..250
FT /evidence="ECO:0007829|PDB:5VYR"
SQ SEQUENCE 259 AA; 29128 MW; DC92E53DE2F8A444 CRC64;
MAIAPNTRVL VAGYGLPAEF CVTTLIGMGV EIDKIAVATH REDNRNCGLH SMLRLRNIQF
TTAAANSEEF YEFGANFDPD MIISMHYRSL IPGRFLKLAK KGSVNLHPSL LPAYRGTNSV
AWVIINGESE TGFSYHRMDE NFDTGAILLQ ERISVEETDT AFSLFHRQIA RAMLRLEEVI
LKLDQGDPGF AQLGEASYYA RELPFGGVID PRWSEVQIDR FIRAMFFPPF PPAVLKIDGK
VYYVPSIDIY RSLMRGIPS
