ALGA_PSEAE
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 03-AUG-2022, entry version 152.
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; Synonyms=pmi; OrderedLocusNames=PA3551;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX 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 (pmi) of
RT Pseudomonas aeruginosa and comparison with the corresponding Escherichia
RT coli gene manA.";
RL Gene 42:293-302(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX 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., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3]
RP PROTEIN SEQUENCE OF 1-10, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=1846611; DOI=10.1016/s0021-9258(18)52212-2;
RA Shinabarger D., Berry A., May T.B., Rothmel R., Fialho A.,
RA Chakrabarty A.M.;
RT "Purification and characterization of phosphomannose isomerase-guanosine
RT diphospho-D-mannose pyrophosphorylase. A bifunctional enzyme in the
RT 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. {ECO:0000269|PubMed:1846611}.
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; Evidence={ECO:0000269|PubMed:1846611};
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 Evidence={ECO:0000269|PubMed:1846611};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:1846611};
CC Note=Co(2+) (for PMI). {ECO:0000269|PubMed:1846611};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.03 mM for D-mannose 6-phosphate {ECO:0000269|PubMed:1846611};
CC KM=20.5 uM for D-mannose 1-phosphate {ECO:0000269|PubMed:1846611};
CC KM=29.5 uM for GTP {ECO:0000269|PubMed:1846611};
CC KM=14.2 uM for GDP-D-mannose {ECO:0000269|PubMed:1846611};
CC Vmax=830 nmol/min/mg enzyme for the PMI forward reaction
CC {ECO:0000269|PubMed:1846611};
CC Vmax=5680 nmol/min/mg enzyme for the GMP forward reaction
CC {ECO:0000269|PubMed:1846611};
CC Vmax=5170 nmol/min/mg enzyme for the GMP reverse reaction
CC {ECO:0000269|PubMed:1846611};
CC pH dependence:
CC Optimum pH is 7.0 for PMI activity, and 7.6 for GMP activity.
CC {ECO:0000269|PubMed:1846611};
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:0000269|PubMed:1846611}.
CC -!- SIMILARITY: Belongs to the mannose-6-phosphate isomerase type 2 family.
CC {ECO:0000305}.
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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; NC_002516.2.
DR RefSeq; WP_003092113.1; NZ_QZGE01000001.1.
DR AlphaFoldDB; P07874; -.
DR SMR; P07874; -.
DR STRING; 287.DR97_4391; -.
DR PaxDb; P07874; -.
DR EnsemblBacteria; AAG06939; AAG06939; PA3551.
DR GeneID; 879142; -.
DR KEGG; pae:PA3551; -.
DR PATRIC; fig|208964.12.peg.3716; -.
DR PseudoCAP; PA3551; -.
DR HOGENOM; CLU_035527_1_0_6; -.
DR InParanoid; P07874; -.
DR OMA; ELKKHDP; -.
DR PhylomeDB; P07874; -.
DR BioCyc; MetaCyc:MON-13384; -.
DR BioCyc; PAER208964:G1FZ6-3619-MON; -.
DR BRENDA; 2.7.7.13; 5087.
DR SABIO-RK; P07874; -.
DR UniPathway; UPA00126; UER00423.
DR UniPathway; UPA00126; UER00930.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004475; F:mannose-1-phosphate guanylyltransferase activity; IDA:PseudoCAP.
DR GO; GO:0004476; F:mannose-6-phosphate isomerase activity; IDA:PseudoCAP.
DR GO; GO:0042121; P:alginic acid biosynthetic process; IMP:PseudoCAP.
DR GO; GO:0009298; P:GDP-mannose biosynthetic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW Alginate biosynthesis; Cobalt; Direct protein sequencing; GTP-binding;
KW Isomerase; Multifunctional enzyme; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..481
FT /note="Alginate biosynthesis protein AlgA"
FT /id="PRO_0000194248"
FT CONFLICT 26..27
FT /note="FL -> LV (in Ref. 1; AAA25972)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="I -> L (in Ref. 1; AAA25972)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="S -> T (in Ref. 1; AAA25972)"
FT /evidence="ECO:0000305"
FT CONFLICT 359..360
FT /note="EV -> DL (in Ref. 1; AAA25972)"
FT /evidence="ECO:0000305"
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
