ALG8_PSEAE
ID ALG8_PSEAE Reviewed; 494 AA.
AC Q52463; Q9HY70;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Mannuronan synthase;
DE EC=2.4.1.33 {ECO:0000269|PubMed:16391057, ECO:0000269|PubMed:18524915};
DE AltName: Full=Glycosyltransferase Alg8;
GN Name=alg8; OrderedLocusNames=PA3541;
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].
RC STRAIN=8830;
RX PubMed=8294014; DOI=10.1016/0378-1119(93)90477-k;
RA Maharaj R., May T.B., Wang S.-K., Chakrabarty A.M.;
RT "Sequence of the alg8 and alg44 genes involved in the synthesis of alginate
RT by Pseudomonas aeruginosa.";
RL Gene 136:267-269(1993).
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 FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=16391057; DOI=10.1128/aem.72.1.298-305.2006;
RA Remminghorst U., Rehm B.H.;
RT "In vitro alginate polymerization and the functional role of Alg8 in
RT alginate production by Pseudomonas aeruginosa.";
RL Appl. Environ. Microbiol. 72:298-305(2006).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=18524915; DOI=10.1099/mic.0.2007/015305-0;
RA Oglesby L.L., Jain S., Ohman D.E.;
RT "Membrane topology and roles of Pseudomonas aeruginosa Alg8 and Alg44 in
RT alginate polymerization.";
RL Microbiology 154:1605-1615(2008).
CC -!- FUNCTION: Processive enzyme that polymerizes GDP-mannuronic acid.
CC {ECO:0000269|PubMed:16391057, ECO:0000269|PubMed:18524915}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-beta-D-mannuronosyl](n) + GDP-alpha-D-mannuronate =
CC [(1->4)-beta-D-mannuronosyl](n+1) + GDP + H(+); Xref=Rhea:RHEA:46876,
CC Rhea:RHEA-COMP:11270, Rhea:RHEA-COMP:11686, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:84886, ChEBI:CHEBI:85311; EC=2.4.1.33;
CC Evidence={ECO:0000269|PubMed:16391057, ECO:0000269|PubMed:18524915};
CC -!- PATHWAY: Glycan biosynthesis; alginate biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC36875.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L22611; AAC36875.2; ALT_INIT; Genomic_DNA.
DR EMBL; AE004091; AAG06929.1; -; Genomic_DNA.
DR PIR; A83204; A83204.
DR RefSeq; NP_252231.1; NC_002516.2.
DR RefSeq; WP_003119545.1; NZ_QZGE01000001.1.
DR AlphaFoldDB; Q52463; -.
DR STRING; 287.DR97_4401; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR TCDB; 4.D.1.1.9; the putative vectorial glycosyl polymerization (vgp) family.
DR PaxDb; Q52463; -.
DR PRIDE; Q52463; -.
DR EnsemblBacteria; AAG06929; AAG06929; PA3541.
DR GeneID; 879005; -.
DR KEGG; pae:PA3541; -.
DR PATRIC; fig|208964.12.peg.3705; -.
DR PseudoCAP; PA3541; -.
DR HOGENOM; CLU_024914_0_0_6; -.
DR InParanoid; Q52463; -.
DR OMA; KLMFRWY; -.
DR PhylomeDB; Q52463; -.
DR BioCyc; MetaCyc:MON-19191; -.
DR BioCyc; PAER208964:G1FZ6-3609-MON; -.
DR UniPathway; UPA00286; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0047643; F:alginate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0050501; F:hyaluronan synthase activity; IBA:GO_Central.
DR GO; GO:0042121; P:alginic acid biosynthetic process; IMP:PseudoCAP.
DR GO; GO:0085029; P:extracellular matrix assembly; IBA:GO_Central.
DR GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; IBA:GO_Central.
DR GO; GO:0030213; P:hyaluronan biosynthetic process; IBA:GO_Central.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Alginate biosynthesis; Cell membrane; Glycosyltransferase; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..494
FT /note="Mannuronan synthase"
FT /id="PRO_0000059254"
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..403
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 423..445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 115
FT /note="A -> R (in Ref. 1; AAC36875)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 494 AA; 56456 MW; D89A5627E913FDF5 CRC64;
MMETYKRGLA EATGWLVFLS LLMVLALAVP KTVFDADSKD FILLIGAVGI WRYSMGGVHF
LRGMLFLHVV YPYYRRRVRQ LGSAADPSHV FLMVTSFRID ALTTAMVYRS VIREAIDSGY
PTTVVCSIVE MSDEVLVRSL WEKMNPPDRV SLDFVRIPGT GKRDGLAYGF RAISRHLPDD
DAVVAVIDGD TVLDHGVVKK TVPWFKLFPN VGGLTTNEFC EVQGGYVMSE WHKLRFAQRH
INMCSMALSK RVLTMTGRMS VFRARVVTNP EFITDVENDH LEHWRLGRFK FLTGDDKSSW
FSLMRLGYDT FYVPDAAINT VEHPPEKSFI KASRKLMYRW YGNNLRQNSR ALKLGARRLG
WFTMLVLFDQ RVSMWTSLLG LVVAILASLK YSIAFLLVYL LWIGLTRLVL TLLLSLSGHR
IGPAYPLILY YNQIVGALVK IYVFFRLDRQ SWTRQPTKLE RGLASFQRWF NAWSSRAMTF
SAASIFVAVL LTIV
