ALGA_PSESM
ID ALGA_PSESM Reviewed; 483 AA.
AC Q887Q9;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Alginate biosynthesis protein AlgA;
DE Includes:
DE RecName: Full=Mannose-6-phosphate isomerase;
DE EC=5.3.1.8;
DE AltName: Full=Phosphohexomutase;
DE AltName: Full=Phosphomannose isomerase;
DE Short=PMI;
DE Includes:
DE RecName: Full=Mannose-1-phosphate guanylyltransferase;
DE EC=2.7.7.13;
DE AltName: Full=GDP-mannose pyrophosphorylase;
DE Short=GMP;
DE Short=GMPP;
DE AltName: Full=GTP--mannose-1-phosphate guanylyltransferase;
GN Name=algA; OrderedLocusNames=PSPTO_1232;
OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=223283;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA Collmer A.;
RT "The complete genome sequence of the Arabidopsis and tomato pathogen
RT Pseudomonas syringae pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
CC -!- FUNCTION: Produces a precursor for alginate polymerization. The
CC alginate layer provides a protective barrier against host immune
CC defenses and antibiotics (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-mannose 6-phosphate = D-fructose 6-phosphate;
CC Xref=Rhea:RHEA:12356, ChEBI:CHEBI:58735, ChEBI:CHEBI:61527;
CC EC=5.3.1.8;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-mannose 1-phosphate + GTP + H(+) = diphosphate + GDP-
CC alpha-D-mannose; Xref=Rhea:RHEA:15229, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57527,
CC ChEBI:CHEBI:58409; EC=2.7.7.13;
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
CC Note=Co(2+) (for PMI). {ECO:0000250};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose
CC biosynthesis; GDP-alpha-D-mannose from alpha-D-mannose 1-phosphate (GTP
CC route): step 1/1.
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose
CC biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate:
CC step 1/2.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the mannose-6-phosphate isomerase type 2 family.
CC {ECO:0000305}.
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DR EMBL; AE016853; AAO54757.1; -; Genomic_DNA.
DR RefSeq; NP_791062.1; NC_004578.1.
DR RefSeq; WP_007244046.1; NC_004578.1.
DR AlphaFoldDB; Q887Q9; -.
DR SMR; Q887Q9; -.
DR STRING; 223283.PSPTO_1232; -.
DR EnsemblBacteria; AAO54757; AAO54757; PSPTO_1232.
DR GeneID; 1182868; -.
DR KEGG; pst:PSPTO_1232; -.
DR PATRIC; fig|223283.9.peg.1253; -.
DR eggNOG; COG0662; Bacteria.
DR eggNOG; COG0836; Bacteria.
DR HOGENOM; CLU_035527_1_0_6; -.
DR OMA; ELKKHDP; -.
DR OrthoDB; 224217at2; -.
DR PhylomeDB; Q887Q9; -.
DR UniPathway; UPA00126; UER00423.
DR UniPathway; UPA00126; UER00930.
DR Proteomes; UP000002515; Chromosome.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004475; F:mannose-1-phosphate guanylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004476; F:mannose-6-phosphate isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0042121; P:alginic acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009298; P:GDP-mannose biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.60.120.10; -; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR006375; Man1P_GuaTrfase/Man6P_Isoase.
DR InterPro; IPR001538; Man6P_isomerase-2_C.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR Pfam; PF01050; MannoseP_isomer; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF51182; SSF51182; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR TIGRFAMs; TIGR01479; GMP_PMI; 1.
PE 3: Inferred from homology;
KW Alginate biosynthesis; Cobalt; GTP-binding; Isomerase;
KW Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..483
FT /note="Alginate biosynthesis protein AlgA"
FT /id="PRO_0000194251"
SQ SEQUENCE 483 AA; 53563 MW; B9EFCA39C452FE44 CRC64;
MIPVILSGGS GSRLWPLSRK QFPKQFLALT GEHTLFQQTL QRLVFEGMQE PIVVCNKDHR
FIVNEQLAAL NLETQAILME PFGRNTAPAV ALTAMKLVNE GNDGLMLVLP ADHVIEDQKA
LQRALALATV TAERGEMVLF GVPANKPETG YGYIKSTADA LLPEGVSRVS QFVEKPDEKR
AKEFVEAGGY YWNSGMFLFR ASRFLEELKK HDPDIYDTCL LTLERSVQDG DALEIDASTF
ACCPDNSIDY AVMEKTQRAC VVPLSAGWSD VGCWSSLWEV NAKDAHGNVT KGDVVIQDSR
NCMIHGNGKL VSVIGLDNIV VVETKDAMMI AHKDKVQGVK QMVATLNEQG RTETQNHLEV
YRPWGSYDSV DMGGRFQVKR ISVKPGACLS LQMHHHRAEH WIVVSGTAQV TCDENVFLLT
ENQSTYIPIA SVHRLRNPGK IPLEIIEVQS GSYLGEDDIE RFEDIYGRSN ALEAGVKTQT
IAR
