ID   GDPPS_VIBCL             Reviewed;         367 AA.
AC   Q06953;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=GDP-perosamine synthase {ECO:0000305};
DE            EC=2.6.1.102 {ECO:0000269|PubMed:11479276};
GN   Name=rfbE {ECO:0000303|PubMed:8529891};
OS   Vibrio cholerae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=666;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=El Tor O17 / Serotype O1;
RX   PubMed=1372980; DOI=10.1073/pnas.89.7.2566;
RA   Stroeher U.H., Karageorgos L.E., Morona R., Manning P.A.;
RT   "Serotype conversion in Vibrio cholerae O1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:2566-2570(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], GENE NAME, AND PATHWAY.
RC   STRAIN=Serotype O1;
RX   PubMed=8529891; DOI=10.1016/0378-1119(95)00589-0;
RA   Stroeher U.H., Karageorgos L.E., Brown M.H., Morona R., Manning P.A.;
RT   "A putative pathway for perosamine biosynthesis is the first function
RT   encoded within the rfb region of Vibrio cholerae O1.";
RL   Gene 166:33-42(1995).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   SUBUNIT.
RC   STRAIN=Serotype O1;
RX   PubMed=11479276; DOI=10.1093/glycob/11.8.655;
RA   Albermann C., Piepersberg W.;
RT   "Expression and identification of the RfbE protein from Vibrio cholerae O1
RT   and its use for the enzymatic synthesis of GDP-D-perosamine.";
RL   Glycobiology 11:655-661(2001).
CC   -!- FUNCTION: Catalyzes the synthesis of GDP-perosamine from GDP-4-keto-6-
CC       deoxy-D-mannose and L-glutamate. Shows also weak activity with L-
CC       glutamine. {ECO:0000269|PubMed:11479276}.
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:11479276};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000269|PubMed:11479276};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.06 mM for GDP-4-keto-6-deoxy-D-mannose
CC         {ECO:0000269|PubMed:11479276};
CC         KM=0.1 mM for L-glutamate {ECO:0000269|PubMed:11479276};
CC       pH dependence:
CC         Optimum pH is 8.0. {ECO:0000269|PubMed:11479276};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC       biosynthesis. {ECO:0000303|PubMed:8529891}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11479276}.
CC   -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family. {ECO:0000305}.
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DR   EMBL; X59554; CAA42137.1; -; Genomic_DNA.
DR   PIR; S28471; S28471.
DR   AlphaFoldDB; Q06953; -.
DR   SMR; Q06953; -.
DR   BioCyc; MetaCyc:MON-13575; -.
DR   UniPathway; UPA00281; -.
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   Transferase.
FT   CHAIN           1..367
FT                   /note="GDP-perosamine synthase"
FT                   /id="PRO_0000430721"
FT   MOD_RES         181
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8ZNF3"
SQ   SEQUENCE   367 AA;  41011 MW;  CA73ABB7CEC5E800 CRC64;
     MIPVYEPSLD GNERKYLNDC IDSGWVSSRG KYIDRFETEF AEFLKVKHAT TVSNGTVALH
     LAMSALGITQ GDEVIVPTFT YVASVNTIVQ CGALPVFAEI EGESLQVSVE DVKRKINKKT
     KAVMAVHIYG QACDIQSLRD LCDEHGLYLI EDCAEAIGTA VNGKKVGTFG DVSTFSFFGN
     KTITSGEGGM VVSNSDIIID KCLRLKNQGV VAGKRYWHDL VAYNYRMTNL CAAIGVAQLE
     RVDKIIKAKR DIAEIYRSEL AGLPMQVHKE SNGTFHSYWL TSIILDQEFE VHRDGLMTFL
     ENNDIESRPF FYPAHTLPMY EHLAEKTAFP LSNSYSHRGI NLPSWPGLCD DQVKEICNCI
     KNYFNCI