GDPPS_ECO57
ID GDPPS_ECO57 Reviewed; 364 AA.
AC Q7DBF3; Q7ACQ1;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=GDP-perosamine synthase {ECO:0000305};
DE EC=2.6.1.102 {ECO:0000269|PubMed:17888872, ECO:0000269|PubMed:18201574};
GN Name=perA {ECO:0000303|PubMed:18201574};
GN Synonyms=per {ECO:0000303|PubMed:17888872},
GN rfbE {ECO:0000303|PubMed:8890241};
GN OrderedLocusNames=Z3200 {ECO:0000312|EMBL:AAG57096.1},
GN ECs2841 {ECO:0000312|EMBL:BAB36264.1};
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
RN [3]
RP DISRUPTION PHENOTYPE, AND PATHWAY.
RC STRAIN=O157:H7 / 86-24 / EHEC;
RX PubMed=8890241; DOI=10.1128/iai.64.11.4795-4801.1996;
RA Bilge S.S., Vary J.C. Jr., Dowell S.F., Tarr P.I.;
RT "Role of the Escherichia coli O157:H7 O side chain in adherence and
RT analysis of an rfb locus.";
RL Infect. Immun. 64:4795-4801(1996).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=O157:H7 / EHEC;
RX PubMed=17888872; DOI=10.1016/j.bbrc.2007.08.184;
RA Zhao G., Liu J., Liu X., Chen M., Zhang H., Wang P.G.;
RT "Cloning and characterization of GDP-perosamine synthetase (Per) from
RT Escherichia coli O157:H7 and synthesis of GDP-perosamine in vitro.";
RL Biochem. Biophys. Res. Commun. 363:525-530(2007).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RC STRAIN=O157:H7 / EHEC;
RX PubMed=18201574; DOI=10.1016/j.febslet.2008.01.005;
RA Albermann C., Beuttler H.;
RT "Identification of the GDP-N-acetyl-d-perosamine producing enzymes from
RT Escherichia coli O157:H7.";
RL FEBS Lett. 582:479-484(2008).
CC -!- FUNCTION: Catalyzes the synthesis of GDP-perosamine from GDP-4-keto-6-
CC deoxy-D-mannose and L-glutamate. Can use only L-glutamate as amino
CC donor. {ECO:0000269|PubMed:17888872, ECO:0000269|PubMed:18201574}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + GDP-alpha-D-perosamine = GDP-4-dehydro-alpha-
CC D-rhamnose + L-glutamate; Xref=Rhea:RHEA:36779, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57964, ChEBI:CHEBI:73996;
CC EC=2.6.1.102; Evidence={ECO:0000269|PubMed:17888872,
CC ECO:0000269|PubMed:18201574};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:17888872, ECO:0000269|PubMed:18201574};
CC -!- ACTIVITY REGULATION: Divalent ions have no significant effect on
CC activity. {ECO:0000269|PubMed:17888872}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.09 mM for GDP-4-keto-6-deoxy-D-mannose
CC {ECO:0000269|PubMed:17888872};
CC KM=0.07 mM for GDP-4-keto-6-deoxy-D-mannose
CC {ECO:0000269|PubMed:18201574};
CC KM=2.0 mM for L-glutamate {ECO:0000269|PubMed:17888872};
CC KM=2.3 mM for L-glutamate {ECO:0000269|PubMed:18201574};
CC Note=kcat is 18.98 sec(-1) for GDP-4-keto-6-deoxy-D-mannose. kcat is
CC 10.41 sec(-1) for L-glutamate. {ECO:0000269|PubMed:17888872};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:17888872,
CC ECO:0000269|PubMed:18201574};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC biosynthesis. {ECO:0000269|PubMed:8890241}.
CC -!- SUBUNIT: Homodecamer. {ECO:0000269|PubMed:17888872,
CC ECO:0000269|PubMed:18201574}.
CC -!- DISRUPTION PHENOTYPE: Mutant is deficient in expression of the O157 LPS
CC antigen. Increases adherence to cultured epithelial cells.
CC {ECO:0000269|PubMed:8890241}.
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB36264.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE005174; AAG57096.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB36264.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_310868.1; NC_002695.1.
DR RefSeq; WP_000875215.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q7DBF3; -.
DR SMR; Q7DBF3; -.
DR STRING; 155864.EDL933_3108; -.
DR EnsemblBacteria; AAG57096; AAG57096; Z3200.
DR EnsemblBacteria; BAB36264; BAB36264; ECs_2841.
DR GeneID; 912508; -.
DR KEGG; ece:Z3200; -.
DR KEGG; ecs:ECs_2841; -.
DR PATRIC; fig|386585.9.peg.2974; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_7_2_6; -.
DR OMA; QVHYKPI; -.
DR BioCyc; MetaCyc:MON-21547; -.
DR UniPathway; UPA00281; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0102933; F:GDP-4-dehydro-6-deoxy-D-mannose-4-aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009243; P:O antigen biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00616; AHBA_syn; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 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 PANTHER; PTHR30244; PTHR30244; 1.
DR Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR PIRSF; PIRSF000390; PLP_StrS; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 1: Evidence at protein level;
KW Aminotransferase; Lipopolysaccharide biosynthesis; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..364
FT /note="GDP-perosamine synthase"
FT /id="PRO_0000430720"
FT MOD_RES 183
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q8ZNF3"
SQ SEQUENCE 364 AA; 41554 MW; BEDF9AAC867C97CD CRC64;
MKYIPVYQPS LTGKEKEYVN ECLDSTWISS KGNYIQKFEN KFAEQNHVQY ATTVSNGTVA
LHLALLALGI SEGDEVIVPT LTYIASVNAI KYTGATPIFV DSDNETWQMS VSDIEQKITN
KTKAIMCVHL YGHPCDMEQI VELAKSRNLF VIEDCAEAFG SKYKGKYVGT FGDISTFSFF
GNKTITTGEG GMVVTNDKTL YDRCLHFKGQ GLAVHRQYWH DVIGYNYRMT NICAAIGLAQ
LEQADDFISR KREIADIYKK NINSLVQVHK ESKDVFHTYW MVSILTRTAE EREELRNHLA
DKLIETRPVF YPVHTMPMYS EKYQKHPIAE DLGWRGINLP SFPSLSNEQV IYICESINEF
YSDK
