ID   ALGA_PSEFL              Reviewed;         483 AA.
AC   P59785;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2003, sequence version 1.
DT   27-MAR-2024, entry version 88.
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;
OS   Pseudomonas fluorescens.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=294;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 17397 / DSM 50091 / CIP 73.25 / NCIMB 10525 / 12;
RX   PubMed=12775688; DOI=10.1128/jb.185.12.3515-3523.2003;
RA   Gimmestad M., Sletta H., Ertesvaag H., Bakkevig K., Jain S., Suh S.-J.,
RA   Skjaak-Braek G., Ellingsen T.E., Ohman D.E., Valla S.;
RT   "The Pseudomonas fluorescens AlgG protein, but not its mannuronan C-5-
RT   epimerase activity, is needed for alginate polymer formation.";
RL   J. Bacteriol. 185:3515-3523(2003).
CC   -!- FUNCTION: Produces a precursor for alginate polymerization. The
CC       alginate layer provides a protective barrier against host immune
CC       defenses and antibiotics.
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; AF527790; AAP46700.1; -; Genomic_DNA.
DR   RefSeq; WP_012722325.1; NZ_CABVHZ010000006.1.
DR   AlphaFoldDB; P59785; -.
DR   SMR; P59785; -.
DR   PATRIC; fig|294.129.peg.5011; -.
DR   eggNOG; COG0662; Bacteria.
DR   eggNOG; COG0836; Bacteria.
DR   UniPathway; UPA00126; UER00423.
DR   UniPathway; UPA00126; UER00930.
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   Transferase.
FT   CHAIN           1..483
FT                   /note="Alginate biosynthesis protein AlgA"
FT                   /id="PRO_0000194249"
SQ   SEQUENCE   483 AA;  53871 MW;  27D861ACA527ECC5 CRC64;
     MIPVILSGGS GSRLWPLSRK QFPKQFLALT GEHTLFQQTL ERLVFEGMDT PIVVCNKDHR
     FIVNEQLANR KLECQRILME PFGRNTAPAV ALTAMMLVNE GRDELMLVLP ADHVIDDQKA
     LQRALALATV AAERGEMVLF GVPATRPETG YGYIKSTNDS LLPEGVSRVQ QFVEKPDEKR
     AVEFVKSGGY FWNSGMFLFR ASRFLEELKK HDPDIYDTCV LTLERSEQTA DTVTLDDATF
     ACCPDNSIDY AVMEKTQRAC VVPLSAGWSD VGCWASLWAV NDKDIHGNVS KGDVVIQDSR
     NCMIHGNGKL VSVIGLDNIV VVETKDAMMI AHKDKVQGVK QMVSTLNDQG RSETQNHCEV
     YRPWGSYDSV DMGGRFQVKH ISVKPGACLS LQMHHHRAEH WIVVSGTAEV TCDENVFLLT
     ENQSTYIPIA SVHRLRNPGK IPLEIIEVQS GSYLGEDDIE RFEDIYGRST PVERGVSVKT
     IAQ
//