GDPPS_CAUVC
ID GDPPS_CAUVC Reviewed; 371 AA.
AC Q9A9H3; O85354;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=GDP-perosamine synthase {ECO:0000303|PubMed:18247575, ECO:0000303|PubMed:18795799};
DE EC=2.6.1.102 {ECO:0000269|PubMed:18247575, ECO:0000269|PubMed:18795799};
GN Name=per {ECO:0000303|PubMed:11390676};
GN OrderedLocusNames=CC_1012 {ECO:0000312|EMBL:AAK22996.1};
OS Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=190650;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=ATCC 19089 / CB15;
RX PubMed=11390676; DOI=10.1099/00221287-147-6-1451;
RA Awram P., Smit J.;
RT "Identification of lipopolysaccharide O antigen synthesis genes required
RT for attachment of the S-layer of Caulobacter crescentus.";
RL Microbiology 147:1451-1460(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19089 / CB15;
RX PubMed=11259647; DOI=10.1073/pnas.061029298;
RA Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT "Complete genome sequence of Caulobacter crescentus.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 2-371, FUNCTION, CATALYTIC
RP ACTIVITY, COFACTOR, AND SUBUNIT.
RX PubMed=18247575; DOI=10.1021/bi702430d;
RA Cook P.D., Holden H.M.;
RT "GDP-perosamine synthase: structural analysis and production of a novel
RT trideoxysugar.";
RL Biochemistry 47:2833-2840(2008).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF MUTANT ALA-186 IN COMPLEX WITH
RP GDP-PEROSAMINE AND WILD-TYPE IN COMPLEX WITH GDP-3-DEOXYPEROSAMINE,
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF LYS-186.
RX PubMed=18795799; DOI=10.1021/bi801309q;
RA Cook P.D., Carney A.E., Holden H.M.;
RT "Accommodation of GDP-linked sugars in the active site of GDP-perosamine
RT synthase.";
RL Biochemistry 47:10685-10693(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. In vitro, can also use GDP-4-keto-3,6-dideoxymannose to produce
CC GDP-3-deoxyperosamine. Involved in the formation of S-LPS, which is
CC required for attachment of the protein S-layer to the outer membrane
CC surface. {ECO:0000269|PubMed:11390676, ECO:0000269|PubMed:18247575,
CC ECO:0000269|PubMed:18795799}.
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:18247575,
CC ECO:0000269|PubMed:18795799};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:18247575, ECO:0000269|PubMed:18795799};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.013 mM for GDP-4-keto-6-deoxy-D-mannose
CC {ECO:0000269|PubMed:18795799};
CC KM=0.016 mM for GDP-4-keto-3,6-dideoxymannose
CC {ECO:0000269|PubMed:18795799};
CC KM=4.6 mM for L-glutamate (with GDP-4-keto-6-deoxy-D-mannose as
CC cosubstrate) {ECO:0000269|PubMed:18795799};
CC KM=0.13 mM for L-glutamate (with GDP-4-keto-3,6-dideoxymannose as
CC cosubstrate) {ECO:0000269|PubMed:18795799};
CC Note=kcat is 2.7 sec(-1) for GDP-4-keto-6-deoxy-D-mannose. kcat is
CC 0.015 sec(-1) for GDP-4-keto-3,6-dideoxymannose.
CC {ECO:0000269|PubMed:18795799};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC biosynthesis. {ECO:0000269|PubMed:11390676}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18247575}.
CC -!- DISRUPTION PHENOTYPE: Mutant produces altered S-LPS.
CC {ECO:0000269|PubMed:11390676}.
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC38670.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF062345; AAC38670.2; ALT_INIT; Genomic_DNA.
DR EMBL; AE005673; AAK22996.1; -; Genomic_DNA.
DR PIR; H87374; H87374.
DR RefSeq; NP_419828.1; NC_002696.2.
DR RefSeq; WP_010918896.1; NC_002696.2.
DR PDB; 3BN1; X-ray; 1.80 A; A/B/C/D=2-371.
DR PDB; 3DR4; X-ray; 1.60 A; A/B/C/D=1-371.
DR PDB; 3DR7; X-ray; 1.70 A; A/B/C/D=1-371.
DR PDBsum; 3BN1; -.
DR PDBsum; 3DR4; -.
DR PDBsum; 3DR7; -.
DR AlphaFoldDB; Q9A9H3; -.
DR SMR; Q9A9H3; -.
DR STRING; 190650.CC_1012; -.
DR EnsemblBacteria; AAK22996; AAK22996; CC_1012.
DR KEGG; ccr:CC_1012; -.
DR PATRIC; fig|190650.5.peg.1030; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_7_2_5; -.
DR OMA; IVNHGMY; -.
DR BioCyc; CAULO:CC1012-MON; -.
DR BRENDA; 2.6.1.102; 1218.
DR UniPathway; UPA00281; -.
DR EvolutionaryTrace; Q9A9H3; -.
DR Proteomes; UP000001816; 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 3D-structure; Aminotransferase; Lipopolysaccharide biosynthesis;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..371
FT /note="GDP-perosamine synthase"
FT /id="PRO_0000430719"
FT MOD_RES 186
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q8ZNF3,
FT ECO:0000303|PubMed:18795799"
FT MUTAGEN 186
FT /note="K->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18795799"
FT HELIX 18..28
FT /evidence="ECO:0007829|PDB:3BN1"
FT HELIX 36..49
FT /evidence="ECO:0007829|PDB:3DR4"
FT STRAND 52..59
FT /evidence="ECO:0007829|PDB:3DR4"
FT HELIX 60..71
FT /evidence="ECO:0007829|PDB:3DR4"
FT STRAND 78..85
FT /evidence="ECO:0007829|PDB:3DR4"
FT HELIX 88..95
FT /evidence="ECO:0007829|PDB:3DR4"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:3DR4"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:3DR4"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:3DR4"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:3DR4"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:3DR4"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:3DR4"
FT HELIX 140..149
FT /evidence="ECO:0007829|PDB:3DR4"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:3DR4"
FT STRAND 173..181
FT /evidence="ECO:0007829|PDB:3DR4"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:3DR4"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:3DR4"
FT HELIX 201..211
FT /evidence="ECO:0007829|PDB:3DR4"
FT HELIX 234..245
FT /evidence="ECO:0007829|PDB:3DR4"
FT HELIX 247..265
FT /evidence="ECO:0007829|PDB:3DR4"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:3DR4"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:3DR4"
FT STRAND 286..292
FT /evidence="ECO:0007829|PDB:3DR4"
FT HELIX 300..309
FT /evidence="ECO:0007829|PDB:3DR4"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:3DR4"
FT HELIX 325..330
FT /evidence="ECO:0007829|PDB:3DR4"
FT HELIX 336..344
FT /evidence="ECO:0007829|PDB:3DR4"
FT STRAND 345..348
FT /evidence="ECO:0007829|PDB:3DR4"
FT HELIX 356..367
FT /evidence="ECO:0007829|PDB:3DR4"
SQ SEQUENCE 371 AA; 40637 MW; AA4205787508C427 CRC64;
MSDLPRISVA APRLDGNERD YVLECMDTTW ISSVGRFIVE FEKAFADYCG VKHAIACNNG
TTALHLALVA MGIGPGDEVI VPSLTYIASA NSVTYCGATP VLVDNDPRTF NLDAAKLEAL
ITPRTKAIMP VHLYGQICDM DPILEVARRH NLLVIEDAAE AVGATYRGKK SGSLGDCATF
SFFGNKIITT GEGGMITTND DDLAAKMRLL RGQGMDPNRR YWFPIVGFNY RMTNIQAAIG
LAQLERVDEH LAARERVVGW YEQKLARLGN RVTKPHVALT GRHVFWMYTV RLGEGLSTTR
DQVIKDLDAL GIESRPVFHP MHIMPPYAHL ATDDLKIAEA CGVDGLNLPT HAGLTEADID
RVIAALDQVL V
