ALD2_RHORT
ID ALD2_RHORT Reviewed; 221 AA.
AC Q2RXI1;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=5-methylthioribulose-1-phosphate/5-deoxyribulose-1-phosphate aldolase {ECO:0000303|PubMed:31950558};
DE EC=4.1.2.62 {ECO:0000269|PubMed:29133429, ECO:0000269|PubMed:31950558};
GN Name=ald2 {ECO:0000303|PubMed:29133429};
GN OrderedLocusNames=Rru_A0359 {ECO:0000312|EMBL:ABC21164.1};
OS Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS NCIMB 8255 / S1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=269796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX PubMed=21886856; DOI=10.4056/sigs.1804360;
RA Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA Mavromatis K., Richardson P., Rohde M., Goeker M., Klenk H.P., Zhang Y.,
RA Roberts G.P., Reslewic S., Schwartz D.C.;
RT "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL Stand. Genomic Sci. 4:293-302(2011).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX PubMed=29133429; DOI=10.1073/pnas.1711625114;
RA North J.A., Miller A.R., Wildenthal J.A., Young S.J., Tabita F.R.;
RT "Microbial pathway for anaerobic 5'-methylthioadenosine metabolism coupled
RT to ethylene formation.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E10455-E10464(2017).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=31950558; DOI=10.1111/mmi.14459;
RA North J.A., Wildenthal J.A., Erb T.J., Evans B.S., Byerly K.M., Gerlt J.A.,
RA Tabita F.R.;
RT "A bifunctional salvage pathway for two distinct S-adenosylmethionine by-
RT products that is widespread in bacteria, including pathogenic Escherichia
RT coli.";
RL Mol. Microbiol. 113:923-937(2020).
CC -!- FUNCTION: Uses 5-methylthioribulose-1-phosphate to yield 2-
CC (methylthio)acetaldehyde and dihydroxyacetone phosphate
CC (PubMed:29133429, PubMed:31950558). Can also use 5-deoxyribulose 1-
CC phosphate to yield acetaldehyde and dihydroxyacetone phosphate
CC (PubMed:31950558). Part of a bifunctional DHAP-shunt salvage pathway
CC for SAM by-products (PubMed:31950558). {ECO:0000269|PubMed:29133429,
CC ECO:0000269|PubMed:31950558}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-methyl-5-thio-D-ribulose 1-phosphate = 2-
CC (methylsulfanyl)acetaldehyde + dihydroxyacetone phosphate;
CC Xref=Rhea:RHEA:56940, ChEBI:CHEBI:57642, ChEBI:CHEBI:58548,
CC ChEBI:CHEBI:141184; EC=4.1.2.62;
CC Evidence={ECO:0000269|PubMed:29133429, ECO:0000269|PubMed:31950558};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56941;
CC Evidence={ECO:0000269|PubMed:31950558};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-deoxy-D-ribulose 1-phosphate = acetaldehyde +
CC dihydroxyacetone phosphate; Xref=Rhea:RHEA:61300, ChEBI:CHEBI:15343,
CC ChEBI:CHEBI:57642, ChEBI:CHEBI:144504; EC=4.1.2.62;
CC Evidence={ECO:0000269|PubMed:31950558};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61301;
CC Evidence={ECO:0000269|PubMed:31950558};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:31950558};
CC Note=Binds 1 cobalt ion per subunit (By similarity). Can also use
CC Ni(2+) (PubMed:31950558). {ECO:0000250|UniProtKB:P0AB87,
CC ECO:0000269|PubMed:31950558};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=288 uM for 5-methylthioribulose-1-phosphate
CC {ECO:0000269|PubMed:31950558};
CC KM=229 uM for 5-deoxyribulose 1-phosphate
CC {ECO:0000269|PubMed:31950558};
CC Note=kcat is 0.94 sec(-1) with 5-methylthioribulose-1-phosphate as
CC substrate. kcat is 1.94 sec(-1) with 5-deoxyribulose 1-phosphate as
CC substrate. kcat is 0.44 sec(-1) with ribulose-1-phosphate as
CC substrate. {ECO:0000269|PubMed:31950558};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage
CC pathway. {ECO:0000305|PubMed:29133429}.
CC -!- DISRUPTION PHENOTYPE: Mutants produce only low levels of ethylene when
CC grown on MTA (PubMed:29133429). Deletion mutant accumulates both S-
CC methyl-5'-thioadenosine and 5'-deoxyadenosine extracellularly
CC (PubMed:31950558). {ECO:0000269|PubMed:29133429,
CC ECO:0000269|PubMed:31950558}.
CC -!- SIMILARITY: Belongs to the aldolase class II family. {ECO:0000305}.
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DR EMBL; CP000230; ABC21164.1; -; Genomic_DNA.
DR RefSeq; WP_011388112.1; NC_007643.1.
DR RefSeq; YP_425451.1; NC_007643.1.
DR AlphaFoldDB; Q2RXI1; -.
DR SMR; Q2RXI1; -.
DR STRING; 269796.Rru_A0359; -.
DR EnsemblBacteria; ABC21164; ABC21164; Rru_A0359.
DR KEGG; rru:Rru_A0359; -.
DR PATRIC; fig|269796.9.peg.415; -.
DR eggNOG; COG0235; Bacteria.
DR HOGENOM; CLU_006033_3_0_5; -.
DR OMA; YATFGTH; -.
DR OrthoDB; 599627at2; -.
DR PhylomeDB; Q2RXI1; -.
DR BioCyc; MetaCyc:MON-21152; -.
DR UniPathway; UPA00904; -.
DR Proteomes; UP000001929; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.225.10; -; 1.
DR InterPro; IPR001303; Aldolase_II/adducin_N.
DR InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR Pfam; PF00596; Aldolase_II; 1.
DR SMART; SM01007; Aldolase_II; 1.
DR SUPFAM; SSF53639; SSF53639; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Cobalt; Lyase; Metal-binding;
KW Methionine biosynthesis; Reference proteome.
FT CHAIN 1..221
FT /note="5-methylthioribulose-1-phosphate/5-deoxyribulose-1-
FT phosphate aldolase"
FT /id="PRO_0000445035"
FT ACT_SITE 75
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0AB87"
FT BINDING 75
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P0AB87"
FT BINDING 94
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P0AB87"
FT BINDING 96
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P0AB87"
FT BINDING 157
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P0AB87"
FT SITE 115
FT /note="Plays a key role in the stabilization of the
FT transition state and positioning the aldehyde component"
FT /evidence="ECO:0000250|UniProtKB:P0AB87"
FT SITE 133
FT /note="Plays a key role in the stabilization of the
FT transition state and positioning the aldehyde component"
FT /evidence="ECO:0000250|UniProtKB:P0AB87"
FT SITE 210
FT /note="Plays a key role in the stabilization of the
FT transition state and positioning the aldehyde component"
FT /evidence="ECO:0000250|UniProtKB:P0AB87"
SQ SEQUENCE 221 AA; 23902 MW; B27049122FB6EF8F CRC64;
MPGSRIALRH GLIDAARQVT TLGLNKGTAG NLSVRAGDGL LITPSGLQAA DLRPNDIVFI
DSEGEWRGPR KPSSEWRFHH DILAERPDVG AVVHTHAPFS TVLACLGRPI PAFHYMVAMA
GGNDIRIGAY ATFGTAELSR HALAAMEGRK ACLLAHHGMI ATGRTLKAAI KLAVEVEELA
EQYWRCLQIA EPEILPADEM ERVLEKFKTY GDNAQLPSPP A
