PSSM_RHILV
ID PSSM_RHILV Reviewed; 300 AA.
AC Q9FCP2;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Exopolysaccharide glucosyl ketal-pyruvate-transferase;
DE EC=2.5.1.98 {ECO:0000269|PubMed:20233262};
GN Name=pssM;
OS Rhizobium leguminosarum bv. viciae.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=387;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=VF39;
RX PubMed=9914965;
RA Sadykov M.R., Ivashina T.V., Kanapin A.A., Shliapnikov M.G.,
RA Ksenzenko V.N.;
RT "Structure-functional organization of exopolysaccharide biosynthetic genes
RT in Rhizobium leguminosarum bv. viciae VF39.";
RL Mol. Biol. (Mosk.) 32:797-804(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=VF39;
RX PubMed=20233262; DOI=10.1111/j.1365-2672.2010.04702.x;
RA Ivashina T.V., Fedorova E.E., Ashina N.P., Kalinchuk N.A., Druzhinina T.N.,
RA Shashkov A.S., Shibaev V.N., Ksenzenko V.N.;
RT "Mutation in the pssM gene encoding ketal pyruvate transferase leads to
RT disruption of Rhizobium leguminosarum bv. viciae-Pisum sativum symbiosis.";
RL J. Appl. Microbiol. 109:731-742(2010).
CC -!- FUNCTION: Catalyzes the pyruvylation of subterminal glucose in the
CC exopolysaccharide (EPS) repeating unit. {ECO:0000269|PubMed:20233262}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[4)-beta-D-GlcA-(1->4)-2-O-Ac-beta-D-GlcA-(1->4)-beta-D-Glc-
CC (1->4)-[3-O-(CH3CH(OH)CH2C(O))-(R)-4,6-CH3(COO(-))C-beta-D-Gal-
CC (1->3)-beta-D-Glc-(1->4)-beta-D-Glc-(1->4)-beta-D-Glc-(1->6)]-2-O-Ac-
CC alpha-DGlc-(1->](n) + n phosphoenolpyruvate = [4)-beta-D-GlcA-(1->4)-
CC 2-O-Ac-beta-D-GlcA-(1->4)-beta-D-Glc-(1->4)-[3-O-(CH3CH(OH)CH2C(O))-
CC (R)-4,6-CH3(COO(-))C-beta-D-Gal-(1->3)-(S)-4,6-CH3(COO(-))C-beta-D-
CC Glc-(1->4)-beta-D-Glc-(1->4)-beta-D-Glc-(1->6)]-2-O-Ac-alpha-DGlc-
CC (1->](n) + n phosphate; Xref=Rhea:RHEA:32087, Rhea:RHEA-COMP:13379,
CC Rhea:RHEA-COMP:14004, ChEBI:CHEBI:43474, ChEBI:CHEBI:58702,
CC ChEBI:CHEBI:63679, ChEBI:CHEBI:138369; EC=2.5.1.98;
CC Evidence={ECO:0000269|PubMed:20233262};
CC -!- PATHWAY: Exopolysaccharide biosynthesis. {ECO:0000269|PubMed:20233262}.
CC -!- DISRUPTION PHENOTYPE: Mutants form aberrant non-nitrogen-fixing nodules
CC on peas. {ECO:0000269|PubMed:20233262}.
CC -!- SIMILARITY: Belongs to the polysaccharide pyruvyl transferase family.
CC {ECO:0000305}.
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DR EMBL; AF028810; AAK77315.1; -; Genomic_DNA.
DR RefSeq; WP_011653111.1; NZ_WIFD01000006.1.
DR AlphaFoldDB; Q9FCP2; -.
DR OMA; AMHGAIV; -.
DR BioCyc; MetaCyc:MON-16995; -.
DR BRENDA; 2.5.1.98; 5343.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR007345; Polysacch_pyruvyl_Trfase.
DR Pfam; PF04230; PS_pyruv_trans; 1.
PE 1: Evidence at protein level;
KW Exopolysaccharide synthesis; Pyruvate; Transferase.
FT CHAIN 1..300
FT /note="Exopolysaccharide glucosyl ketal-pyruvate-
FT transferase"
FT /id="PRO_0000418821"
SQ SEQUENCE 300 AA; 34182 MW; C8A9BB4BE1A03A66 CRC64;
MKMFAYRGKH ENFGDELNHW LWERLLPGFF DEDESQLFLG IGSILYDNFD PNMQKIVFGS
GYGGYTNPPK VDGNWTFYFV RGKKTAEVLG IDPSYAIGDS GILTRSCWDA KSIEKRYPVS
FMPHYESAMY GSWDKVCELA GIHYIDPRWP VEKVLTEISA SHKVVSEAMH GCIISDALRV
PWRAIRPIAP GNRAKWYDWA SALDLEIDFD PIGPSNVVEA GASLVRNNTY LLKNITFRHR
RIRQLTGNYV FGSTVKTLQR VAEKPGQLSS DESMVNAHNR MLLELDRLKQ DFSKKTASVL
