WECE_ECOLI
ID WECE_ECOLI Reviewed; 376 AA.
AC P27833; Q2M899;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=dTDP-4-amino-4,6-dideoxygalactose transaminase {ECO:0000255|HAMAP-Rule:MF_02026, ECO:0000305};
DE EC=2.6.1.59 {ECO:0000255|HAMAP-Rule:MF_02026, ECO:0000269|PubMed:15271350};
GN Name=wecE {ECO:0000255|HAMAP-Rule:MF_02026, ECO:0000303|PubMed:15271350};
GN Synonyms=rffA {ECO:0000303|PubMed:8366065}, yifI;
GN OrderedLocusNames=b3791, JW3765;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=1379743; DOI=10.1126/science.1379743;
RA Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
RT "Analysis of the Escherichia coli genome: DNA sequence of the region from
RT 84.5 to 86.5 minutes.";
RL Science 257:771-778(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP C-TERMINUS.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP PATHWAY, AND DISRUPTION PHENOTYPE.
RX PubMed=2166030; DOI=10.1016/s0021-9258(18)77373-0;
RA Meier-Dieter U., Starman R., Barr K., Mayer H., Rick P.D.;
RT "Biosynthesis of enterobacterial common antigen in Escherichia coli.
RT Biochemical characterization of Tn10 insertion mutants defective in
RT enterobacterial common antigen synthesis.";
RL J. Biol. Chem. 265:13490-13497(1990).
RN [5]
RP IDENTIFICATION.
RX PubMed=8366065; DOI=10.1128/jb.175.17.5738-5739.1993;
RA Barr K., Rick P.D.;
RT "Physical map location of the rffC and rffA genes of Escherichia coli.";
RL J. Bacteriol. 175:5738-5739(1993).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RC STRAIN=K12;
RX PubMed=15271350; DOI=10.1016/j.chembiol.2004.04.015;
RA Hwang B.Y., Lee H.J., Yang Y.H., Joo H.S., Kim B.G.;
RT "Characterization and investigation of substrate specificity of the sugar
RT aminotransferase WecE from E. coli K12.";
RL Chem. Biol. 11:915-925(2004).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.24 ANGSTROMS).
RA Wang F., Singh S., Cao H., Xu W., Miller M.D., Thorson J.S.,
RA Phillips G.N. Jr.;
RT "Crystal structure of sugar aminotransferase WecE with external aldimine
RT VII from Escherichia coli K-12.";
RL Submitted (SEP-2014) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the synthesis of dTDP-4-amino-4,6-dideoxy-D-
CC galactose (dTDP-Fuc4N) from dTDP-4-keto-6-deoxy-D-glucose (dTDP-D-
CC Glc4O) and L-glutamate. {ECO:0000255|HAMAP-Rule:MF_02026,
CC ECO:0000269|PubMed:15271350}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + dTDP-4-amino-4,6-dideoxy-alpha-D-galactose =
CC dTDP-4-dehydro-6-deoxy-alpha-D-glucose + L-glutamate;
CC Xref=Rhea:RHEA:10368, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:57649, ChEBI:CHEBI:68492; EC=2.6.1.59;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02026,
CC ECO:0000269|PubMed:15271350};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02026,
CC ECO:0000269|PubMed:15271350};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.11 mM for TDP-4-keto-6-deoxy-D-glucose
CC {ECO:0000269|PubMed:15271350};
CC Note=kcat is 0.38 sec(-1). {ECO:0000269|PubMed:15271350};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:15271350};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:15271350};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; enterobacterial common
CC antigen biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02026,
CC ECO:0000269|PubMed:2166030}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:15271350}.
CC -!- DISRUPTION PHENOTYPE: Mutants do not synthesize TDP-Fuc4NAc and
CC enterobacterial common antigen (ECA). {ECO:0000269|PubMed:2166030}.
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family. {ECO:0000255|HAMAP-
CC Rule:MF_02026, ECO:0000305}.
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DR EMBL; M87049; AAA67591.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAC76796.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77507.1; -; Genomic_DNA.
DR PIR; B65183; B65183.
DR RefSeq; NP_418238.1; NC_000913.3.
DR RefSeq; WP_000612043.1; NZ_SSZK01000025.1.
DR PDB; 4PIW; X-ray; 2.70 A; A/B/C/D/E/F/G/H=1-376.
DR PDB; 4ZAH; X-ray; 2.24 A; A/B/C/D/E/F/G/H=1-376.
DR PDBsum; 4PIW; -.
DR PDBsum; 4ZAH; -.
DR AlphaFoldDB; P27833; -.
DR SMR; P27833; -.
DR BioGRID; 4263175; 300.
DR IntAct; P27833; 4.
DR STRING; 511145.b3791; -.
DR jPOST; P27833; -.
DR PaxDb; P27833; -.
DR PRIDE; P27833; -.
DR DNASU; 948296; -.
DR EnsemblBacteria; AAC76796; AAC76796; b3791.
DR EnsemblBacteria; BAE77507; BAE77507; BAE77507.
DR GeneID; 948296; -.
DR KEGG; ecj:JW3765; -.
DR KEGG; eco:b3791; -.
DR PATRIC; fig|1411691.4.peg.2915; -.
DR EchoBASE; EB1425; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_0_2_6; -.
DR InParanoid; P27833; -.
DR OMA; CQHNAHM; -.
DR PhylomeDB; P27833; -.
DR BioCyc; EcoCyc:RFFTRANS-MON; -.
DR BioCyc; MetaCyc:RFFTRANS-MON; -.
DR BRENDA; 2.6.1.33; 2026.
DR BRENDA; 2.6.1.59; 2026.
DR UniPathway; UPA00566; -.
DR PRO; PR:P27833; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0019180; F:dTDP-4-amino-4,6-dideoxygalactose transaminase activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:EcoCyc.
DR GO; GO:0008483; F:transaminase activity; IBA:GO_Central.
DR GO; GO:0009246; P:enterobacterial common antigen biosynthetic process; IMP:EcoCyc.
DR GO; GO:0000271; P:polysaccharide biosynthetic process; IBA:GO_Central.
DR CDD; cd00616; AHBA_syn; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_02026; WecE_RffA; 1.
DR InterPro; IPR000653; DegT/StrS_aminotransferase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR032894; WecE.
DR InterPro; IPR012749; WecE-like.
DR PANTHER; PTHR30244; PTHR30244; 1.
DR Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR PIRSF; PIRSF000390; PLP_StrS; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR02379; ECA_wecE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..376
FT /note="dTDP-4-amino-4,6-dideoxygalactose transaminase"
FT /id="PRO_0000110016"
FT MOD_RES 181
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q8ZNF3, ECO:0000255|HAMAP-
FT Rule:MF_02026"
FT HELIX 13..23
FT /evidence="ECO:0007829|PDB:4ZAH"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:4PIW"
FT HELIX 31..44
FT /evidence="ECO:0007829|PDB:4ZAH"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:4ZAH"
FT HELIX 55..65
FT /evidence="ECO:0007829|PDB:4ZAH"
FT STRAND 73..80
FT /evidence="ECO:0007829|PDB:4ZAH"
FT HELIX 82..89
FT /evidence="ECO:0007829|PDB:4ZAH"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:4ZAH"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:4ZAH"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:4ZAH"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:4ZAH"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:4ZAH"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:4ZAH"
FT HELIX 135..144
FT /evidence="ECO:0007829|PDB:4ZAH"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:4ZAH"
FT STRAND 168..176
FT /evidence="ECO:0007829|PDB:4ZAH"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:4ZAH"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:4PIW"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:4ZAH"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:4ZAH"
FT HELIX 200..207
FT /evidence="ECO:0007829|PDB:4ZAH"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:4PIW"
FT HELIX 237..248
FT /evidence="ECO:0007829|PDB:4ZAH"
FT HELIX 250..273
FT /evidence="ECO:0007829|PDB:4ZAH"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:4PIW"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:4ZAH"
FT HELIX 300..312
FT /evidence="ECO:0007829|PDB:4ZAH"
FT TURN 324..326
FT /evidence="ECO:0007829|PDB:4PIW"
FT HELIX 328..333
FT /evidence="ECO:0007829|PDB:4ZAH"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:4ZAH"
FT HELIX 343..349
FT /evidence="ECO:0007829|PDB:4ZAH"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:4ZAH"
FT HELIX 361..374
FT /evidence="ECO:0007829|PDB:4ZAH"
SQ SEQUENCE 376 AA; 41901 MW; 22936C67822D1844 CRC64;
MIPFNAPPVV GTELDYMQSA MGSGKLCGDG GFTRRCQQWL EQRFGSAKVL LTPSCTASLE
MAALLLDIQP GDEVIMPSYT FVSTANAFVL RGAKIVFVDV RPDTMNIDET LIEAAITDKT
RVIVPVHYAG VACEMDTIMA LAKKHNLFVV EDAAQGVMST YKGRALGTIG HIGCFSFHET
KNYTAGGEGG ATLINDKALI ERAEIIREKG TNRSQFFRGQ VDKYTWRDIG SSYLMSDLQA
AYLWAQLEAA DRINQQRLAL WQNYYDALAP LAKAGRIELP SIPDGCVQNA HMFYIKLRDI
DDRSALINFL KEAEIMAVFH YIPLHGCPAG EHFGEFHGED RYTTKESERL LRLPLFYNLS
PVNQRTVIAT LLNYFS
