ALG44_PSEAE
ID ALG44_PSEAE Reviewed; 389 AA.
AC Q9HY69; Q52464; Q5EI78;
DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Mannuronan synthase;
DE EC=2.4.1.33 {ECO:0000269|PubMed:18524915};
DE AltName: Full=Alginate biosynthesis protein Alg44;
GN Name=alg44; OrderedLocusNames=PA3542;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-282.
RA Muhammadi A.N.;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP ROLE IN ALGINATE PRODUCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=FRD1;
RX PubMed=16797016; DOI=10.1016/j.febslet.2006.05.077;
RA Remminghorst U., Rehm B.H.A.;
RT "Alg44, a unique protein required for alginate biosynthesis in Pseudomonas
RT aeruginosa.";
RL FEBS Lett. 580:3883-3888(2006).
RN [5]
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: Required for alginate biosynthesis.
CC {ECO:0000269|PubMed:16797016, 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:18524915};
CC -!- PATHWAY: Glycan biosynthesis; alginate biosynthesis.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:16797016}.
CC -!- SIMILARITY: Belongs to the Alg44 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC36876.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L22611; AAC36876.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AE004091; AAG06930.1; -; Genomic_DNA.
DR EMBL; AY880026; AAW77927.1; -; Genomic_DNA.
DR PIR; C83202; C83202.
DR RefSeq; NP_252232.1; NC_002516.2.
DR RefSeq; WP_003092101.1; NZ_QZGE01000001.1.
DR PDB; 4RT0; X-ray; 1.80 A; A/B/C=14-122.
DR PDB; 4RT1; X-ray; 1.70 A; A/B/C=14-122.
DR PDB; 4XRN; X-ray; 2.00 A; A/B/C/D=16-122.
DR PDBsum; 4RT0; -.
DR PDBsum; 4RT1; -.
DR PDBsum; 4XRN; -.
DR AlphaFoldDB; Q9HY69; -.
DR SMR; Q9HY69; -.
DR STRING; 287.DR97_4400; -.
DR PaxDb; Q9HY69; -.
DR DNASU; 878770; -.
DR EnsemblBacteria; AAG06930; AAG06930; PA3542.
DR GeneID; 878770; -.
DR KEGG; pae:PA3542; -.
DR PATRIC; fig|208964.12.peg.3706; -.
DR PseudoCAP; PA3542; -.
DR HOGENOM; CLU_058768_0_0_6; -.
DR OMA; RFSYRQF; -.
DR PhylomeDB; Q9HY69; -.
DR BioCyc; MetaCyc:MON-19192; -.
DR BioCyc; PAER208964:G1FZ6-3610-MON; -.
DR UniPathway; UPA00286; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0009276; C:Gram-negative-bacterium-type cell wall; IDA:PseudoCAP.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0047643; F:alginate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0035438; F:cyclic-di-GMP binding; IEA:InterPro.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IDA:PseudoCAP.
DR GO; GO:0042121; P:alginic acid biosynthetic process; IDA:PseudoCAP.
DR GO; GO:0044010; P:single-species biofilm formation; IDA:PseudoCAP.
DR InterPro; IPR009875; PilZ_domain.
DR Pfam; PF07238; PilZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alginate biosynthesis; Glycosyltransferase; Periplasm;
KW Reference proteome; Transferase.
FT CHAIN 1..389
FT /note="Mannuronan synthase"
FT /id="PRO_0000064552"
FT DOMAIN 16..116
FT /note="PilZ"
FT CONFLICT 172
FT /note="G -> S (in Ref. 1; AAC36876)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="G -> A (in Ref. 1; AAC36876)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="G -> A (in Ref. 1; AAC36876)"
FT /evidence="ECO:0000305"
FT STRAND 25..31
FT /evidence="ECO:0007829|PDB:4RT0"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:4RT0"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:4RT0"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:4RT0"
FT STRAND 64..73
FT /evidence="ECO:0007829|PDB:4RT0"
FT STRAND 76..89
FT /evidence="ECO:0007829|PDB:4RT0"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:4RT0"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:4RT0"
FT HELIX 105..121
FT /evidence="ECO:0007829|PDB:4RT0"
SQ SEQUENCE 389 AA; 41787 MW; 43C09F727FA6A5E5 CRC64;
MNTAVNVNVV HESEAQRQFA RVKLPARIRY IGANREGVDA RLLDLSAGGF AFTASGAPIQ
PGDLYKGKLL FQVDSISFSL EVEFQVRSVD PASRRVGCEF QNLKPREVAA LRYLITSYLA
GEVIGVGDML NTLQRENFTK ARKQGGGNGG MGFFGRVRAV TLSTAIFVVG VGAFAFILNQ
MYNLYFVTHA DSGVVSVPNQ QITMPREGTV QSLLGPNAEV AKGAPIATFS ANLLDMLKGN
LTEEQLNPGN IEKLFGHQMK GTLTSPCDCR VVQQLVADGQ YANKGQVIFT LAPRDSVASI
EARFPYRNAA ELAPGTRVNF QVAGDGVNRS GRIVNTAPVD GDLSSEIRVQ IQPDQPLDAQ
YAGRPAEVSI GGLPGRTLLN KAVTLATAR
