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   27-MAR-2024, entry version 119.
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; Pseudomonadota; 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   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   OrthoDB; 9806359at2; -.
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 (GTP) 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   CDD; cd02213; cupin_PMI_typeII_C; 1.
DR   CDD; cd02509; GDP-M1P_Guanylyltransferase; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   InterPro; IPR049577; GMPP_N.
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   NCBIfam; TIGR01479; GMP_PMI; 1.
DR   PANTHER; PTHR46390; MANNOSE-1-PHOSPHATE GUANYLYLTRANSFERASE; 1.
DR   PANTHER; PTHR46390:SF1; MANNOSE-1-PHOSPHATE GUANYLYLTRANSFERASE; 1.
DR   Pfam; PF01050; MannoseP_isomer; 1.
DR   Pfam; PF00483; NTP_transferase; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   SUPFAM; SSF51182; RmlC-like cupins; 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
//