MANB_SALTY
ID MANB_SALTY Reviewed; 456 AA.
AC P26341;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Phosphomannomutase;
DE Short=PMM;
DE EC=5.4.2.8;
GN Name=manB; Synonyms=cpsG, rfbL; OrderedLocusNames=STM2104;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=1712067; DOI=10.1007/bf00259668;
RA Stevenson G., Lee S.J., Romana L.K., Reeves P.R.;
RT "The cps gene cluster of Salmonella strain LT2 includes a second mannose
RT pathway: sequence of two genes and relationship to genes in the rfb gene
RT cluster.";
RL Mol. Gen. Genet. 227:173-180(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
CC -!- FUNCTION: Involved in the biosynthesis of the capsular polysaccharide
CC colanic acid.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate;
CC Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735;
CC EC=5.4.2.8;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose
CC biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate:
CC step 2/2.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
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DR EMBL; X59886; CAA42541.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21008.1; -; Genomic_DNA.
DR PIR; S16291; S16291.
DR RefSeq; NP_461049.1; NC_003197.2.
DR RefSeq; WP_000164218.1; NC_003197.2.
DR AlphaFoldDB; P26341; -.
DR SMR; P26341; -.
DR STRING; 99287.STM2104; -.
DR PaxDb; P26341; -.
DR PRIDE; P26341; -.
DR EnsemblBacteria; AAL21008; AAL21008; STM2104.
DR GeneID; 1253625; -.
DR KEGG; stm:STM2104; -.
DR PATRIC; fig|99287.12.peg.2226; -.
DR HOGENOM; CLU_016950_9_2_6; -.
DR OMA; KCSQVMY; -.
DR PhylomeDB; P26341; -.
DR BioCyc; SENT99287:STM2104-MON; -.
DR UniPathway; UPA00126; UER00424.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0009298; P:GDP-mannose biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR InterPro; IPR005845; A-D-PHexomutase_a/b/a-II.
DR InterPro; IPR005846; A-D-PHexomutase_a/b/a-III.
DR InterPro; IPR005843; A-D-PHexomutase_C.
DR InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF02880; PGM_PMM_III; 1.
DR Pfam; PF00408; PGM_PMM_IV; 1.
DR PRINTS; PR00509; PGMPMM.
DR SUPFAM; SSF53738; SSF53738; 3.
DR SUPFAM; SSF55957; SSF55957; 1.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
KW Capsule biogenesis/degradation; Isomerase; Lipopolysaccharide biosynthesis;
KW Magnesium; Metal-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..456
FT /note="Phosphomannomutase"
FT /id="PRO_0000147822"
FT ACT_SITE 98
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 249
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT CONFLICT 55..56
FT /note="KL -> NV (in Ref. 1; CAA42541)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 456 AA; 50002 MW; 6E32422242AF2CE2 CRC64;
MTKLTCFKAY DIRGRLGEEL NEDIAWRIGR AYGEYLKPKT VVLGGDVRLT SEALKLALAK
GLQDAGVDVL DIGMSGTEEI YFATFHLGVD GGIEVTASHN PMDYNGMKLV REGARPISGD
TGLRDVQRLA EAGDFPPVNE AARGSYRQIS LRDAYIDHLL GYISVNNLTP LKLVFNAGNG
AAGPVIDAIE ARLKALGAPV EFIKIHNTPD GTFPNGIPNP LLPECRDDTR KAVIEHGADM
GIAFDGDFDR CFLFDEKGQF IEGYYIVGLL AEAFLEKHPG AKIIHDPRLT WNTEAVVTAA
GGTPVMSKTG HAFIKERMRT EDAIYGGEMS AHHYFRDFAY CDSGMIPWLL VAELVCLKRQ
SLGELVRDRM AAFPASGEIN SRLAEPAAAI ARVEAHFAEE AQAVDRTDGL SMSFADWRFN
LRSSNTEPVV RLNVESRGDI PLMEARTRTL LALLNQ
