ID   ALGA_PSEPK              Reviewed;         485 AA.
AC   Q88ND5;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=PP_1277;
OS   Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS   / KT2440).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX   PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA   Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA   Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA   Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA   Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA   Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA   Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA   Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA   Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT   "Complete genome sequence and comparative analysis of the metabolically
RT   versatile Pseudomonas putida KT2440.";
RL   Environ. Microbiol. 4:799-808(2002).
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; AE015451; AAN66901.1; -; Genomic_DNA.
DR   RefSeq; NP_743437.1; NC_002947.4.
DR   AlphaFoldDB; Q88ND5; -.
DR   SMR; Q88ND5; -.
DR   STRING; 160488.PP_1277; -.
DR   EnsemblBacteria; AAN66901; AAN66901; PP_1277.
DR   KEGG; ppu:PP_1277; -.
DR   PATRIC; fig|160488.4.peg.1354; -.
DR   eggNOG; COG0662; Bacteria.
DR   eggNOG; COG0836; Bacteria.
DR   HOGENOM; CLU_035527_1_0_6; -.
DR   OMA; ELKKHDP; -.
DR   PhylomeDB; Q88ND5; -.
DR   BioCyc; PPUT160488:G1G01-1364-MON; -.
DR   UniPathway; UPA00126; UER00423.
DR   UniPathway; UPA00126; UER00930.
DR   Proteomes; UP000000556; 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..485
FT                   /note="Alginate biosynthesis protein AlgA"
FT                   /id="PRO_0000194250"
SQ   SEQUENCE   485 AA;  53896 MW;  81668C8ED0E2A90C CRC64;
     MMIPVILSGG SGSRLWPLSR KQFPKQFLAL TGEHTLFQQT IERLVFEGMD TPIVVCNKDH
     KFIVQEQLAA LKLETQGILM EPFGRNTAPA VAMAAMKLVN EGRDELMLVL PADHVIDDQK
     ALQRALALAT VAAERGEMVL FGVPATKPET GYGYIRSSQD ALLPEGVARV AQFVEKPDEK
     RAAEFVQAGG YFWNSGMFLF RASRFLEELK KHDGDIYDTC VLALERSQED GDVLSIDEAT
     FACCPDNSID YAVMEKTQRA CVVPMSAGWS DVGCWSSLWE VHEKDDNGNV TKGDVVVQDS
     RNCMIHGNGK LVSVIGLENI VVVETKDAMM IAHKDKVQGV KQMVKTLDEQ GRTETQNHLE
     VYRPWGSYDS VDMGGRFQVK HITVKPGASL SLQMHHHRAE HWIVVSGTAE VTCDENVFLL
     TENQSTYIPI ASVHRLRNPG KIPLEIIEVQ SGSYLGEDDI ERFEDVYGRT STPIERGVSV
     KTIAQ