ID   ALGA_PSEAE              Reviewed;         481 AA.
AC   P07874; Q9HY66;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 3.
DT   16-JUN-2009, entry version 80.
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=Phosphomannose isomerase;
DE              Short=PMI;
DE     AltName: Full=Phosphohexomutase;
DE   Includes:
DE     RecName: Full=Mannose-1-phosphate guanylyltransferase;
DE              EC=2.7.7.13;
DE     AltName: Full=GDP-mannose pyrophosphorylase;
DE              Short=GMPP;
DE              Short=GMP;
DE     AltName: Full=GTP--mannose-1-phosphate guanylyltransferase;
GN   Name=algA; Synonyms=pmi; OrderedLocusNames=PA3551;
OS   Pseudomonas aeruginosa.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=86276004; PubMed=3089876; DOI=10.1016/0378-1119(86)90233-7;
RA   Darzins A., Frantz B., Vanags R.I., Chakrabarty A.M.;
RT   "Nucleotide sequence analysis of the phosphomannose isomerase gene
RT   (pmi) of Pseudomonas aeruginosa and comparison with the corresponding
RT   Escherichia coli gene manA.";
RL   Gene 42:293-302(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;
RX   MEDLINE=20437337; PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T.,
RA   Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an
RT   opportunistic pathogen.";
RL   Nature 406:959-964(2000).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-10, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT,
RP   COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   MEDLINE=91115815; PubMed=1846611;
RA   Shinabarger D., Berry A., May T.B., Rothmel R., Fialho A.,
RA   Chakrabarty A.M.;
RT   "Purification and characterization of phosphomannose isomerase-
RT   guanosine diphospho-D-mannose pyrophosphorylase. A bifunctional enzyme
RT   in the alginate biosynthetic pathway of Pseudomonas aeruginosa.";
RL   J. Biol. Chem. 266:2080-2088(1991).
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: D-mannose 6-phosphate = D-fructose 6-
CC       phosphate.
CC   -!- CATALYTIC ACTIVITY: GTP + alpha-D-mannose 1-phosphate =
CC       diphosphate + GDP-mannose.
CC   -!- COFACTOR: Cobalt (for PMI).
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=3.03 mM for D-mannose 6-phosphate;
CC         KM=20.5 uM for D-mannose 1-phosphate;
CC         KM=29.5 uM for GTP;
CC         KM=14.2 uM for GDP-D-mannose;
CC         Vmax=830 nmol/min/mg enzyme for the PMI forward reaction;
CC         Vmax=5680 nmol/min/mg enzyme for the GMP forward reaction;
CC         Vmax=5170 nmol/min/mg enzyme for the GMP reverse reaction;
CC       pH dependence:
CC         Optimum pH is 7.0 for PMI activity, and 7.6 for GMP activity;
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-D-mannose
CC       biosynthesis; GDP-D-mannose from alpha-D-mannose 1-phosphate (GTP
CC       route): step 1/1.
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-D-mannose
CC       biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-
CC       phosphate: step 1/2.
CC   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the mannose-6-phosphate isomerase type 2
CC       family.
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DR   EMBL; M14037; AAA25972.1; -; Genomic_DNA.
DR   EMBL; AE004091; AAG06939.1; -; Genomic_DNA.
DR   PIR; A38598; A38598.
DR   PIR; B83201; B83201.
DR   RefSeq; NP_252241.1; -.
DR   GeneID; 879142; -.
DR   GenomeReviews; AE004091_GR; PA3551.
DR   KEGG; pae:PA3551; -.
DR   PseudoCAP; PA3551; -.
DR   HOGENOM; P07874; -.
DR   OMA; P07874; AEHRMVA.
DR   BioCyc; MetaCyc:MON-13384; -.
DR   BioCyc; PAER208964:PA3551-MON; -.
DR   BRENDA; 2.7.7.13; 354.
DR   BRENDA; 2.7.7.22; 354.
DR   BRENDA; 5.3.1.8; 354.
DR   GO; GO:0050897; F:cobalt ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004475; F:mannose-1-phosphate guanylyltransferase act...; IEA:EC.
DR   GO; GO:0004476; F:mannose-6-phosphate isomerase activity; IEA:EC.
DR   GO; GO:0042121; P:alginic acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:InterPro.
DR   InterPro; IPR006375; Man1P_GuaTrfase/Man6P_Isoase.
DR   InterPro; IPR001538; Man6P_isomerase-2_C.
DR   InterPro; IPR005835; NTP_transferase.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   Gene3D; G3DSA:2.60.120.10; RmlC-like_jellyroll; 1.
DR   Pfam; PF01050; MannoseP_isomer; 1.
DR   Pfam; PF00483; NTP_transferase; 1.
DR   ProDom; PD002664; Man6P_isomerII; 1.
DR   TIGRFAMs; TIGR01479; GMP_PMI; 1.
PE   1: Evidence at protein level;
KW   Alginate biosynthesis; Cobalt; Complete proteome;
KW   Direct protein sequencing; GTP-binding; Isomerase;
KW   Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase;
KW   Transferase.
FT   CHAIN         1    481       Alginate biosynthesis protein algA.
FT                                /FTId=PRO_0000194248.
FT   CONFLICT     26     27       FL -> LV (in Ref. 1; AAA25972).
FT   CONFLICT    115    115       I -> L (in Ref. 1; AAA25972).
FT   CONFLICT    157    157       S -> T (in Ref. 1; AAA25972).
FT   CONFLICT    359    360       EV -> DL (in Ref. 1; AAA25972).
SQ   SEQUENCE   481 AA;  53128 MW;  2D497AF9059AEF97 CRC64;
     MIPVILSGGS GSRLWPLSRK QYPKQFLALT GDDTLFQQTI KRLAFDGMQA PLLVCNKEHR
     FIVQEQLEAQ NLASQAILLE PFGRNTAPAV AIAAMKLVAE GRDELLLILP ADHVIEDQRA
     FQQALALATN AAEKGEMVLF GIPASRPETG YGYIRASADA QLPEGVSRVQ SFVEKPDEAR
     AREFVAAGGY YWNSGMFLFR ASRYLEELKK HDADIYDTCL LALERSQHDG DLVNIDAATF
     ECCPDNSIDY AVMEKTSRAC VVPLSAGWND VGSWSSIWDV HAKDANGNVT KGDVLVHDSH
     NCLVHGNGKL VSVIGLEDIV VVETKDAMMI AHKDRVQDVK HVVKDLDAQG RSETQNHCEV
     YRPWGSYDSV DMGGRFQVKH ITVKPGARLS LQMHHHRAEH WIVVSGTAQV TCDDKTFLLT
     ENQSTYIPIA SVHRLANPGK IPLEIIEVQS GSYLGEDDIE RLEDVYGRTA EPALQVVAGS
     R
//