ALGA_PSEFL
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 25-MAY-2022, entry version 82.
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; Proteobacteria; 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 STRING; 690597.JH730975_gene4177; -.
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 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 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
