RLP_RHORT
ID RLP_RHORT Reviewed; 374 AA.
AC Q2RSU7;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=5-methylthioribulose-1-phosphate isomerase {ECO:0000305};
DE EC=5.3.3.23 {ECO:0000269|PubMed:18826254};
GN Name=rlp {ECO:0000303|PubMed:23042035};
GN OrderedLocusNames=Rru_A1998 {ECO:0000312|EMBL:ABC22798.1};
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, AND DISRUPTION PHENOTYPE.
RX PubMed=18826254; DOI=10.1021/bi801685f;
RA Imker H.J., Singh J., Warlick B.P., Tabita F.R., Gerlt J.A.;
RT "Mechanistic diversity in the RuBisCO superfamily: a novel isomerization
RT reaction catalyzed by the RuBisCO-like protein from Rhodospirillum
RT rubrum.";
RL Biochemistry 47:11171-11173(2008).
RN [3]
RP FUNCTION, PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX PubMed=23042035; DOI=10.1038/nchembio.1087;
RA Erb T.J., Evans B.S., Cho K., Warlick B.P., Sriram J., Wood B.M.,
RA Imker H.J., Sweedler J.V., Tabita F.R., Gerlt J.A.;
RT "A RubisCO-like protein links SAM metabolism with isoprenoid
RT biosynthesis.";
RL Nat. Chem. Biol. 8:926-932(2012).
RN [4]
RP 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).
CC -!- FUNCTION: Catalyzes the conversion of 5-methylthio-D-ribulose 1-
CC phosphate (MTRu-1P) to a 3:1 mixture of 1-methylthioxylulose 5-
CC phosphate (MTXu-5P) and 1-methylthioribulose 5-phosphate (MTRu-5P)
CC (PubMed:18826254). Involved in the MTA-isoprenoid shunt of the
CC methionine salvage pathway (PubMed:23042035).
CC {ECO:0000269|PubMed:18826254, ECO:0000269|PubMed:23042035}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-methyl-5-thio-D-ribulose 1-phosphate = S-methyl-1-thio-D-
CC xylulose 5-phosphate; Xref=Rhea:RHEA:57100, ChEBI:CHEBI:58548,
CC ChEBI:CHEBI:141466; EC=5.3.3.23;
CC Evidence={ECO:0000269|PubMed:18826254};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-methyl-5-thio-D-ribulose 1-phosphate = S-methyl-1-thiol-D-
CC ribulose 5-phosphate; Xref=Rhea:RHEA:57580, ChEBI:CHEBI:58548,
CC ChEBI:CHEBI:85606; EC=5.3.3.23;
CC Evidence={ECO:0000269|PubMed:18826254};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage
CC pathway. {ECO:0000305|PubMed:29133429}.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; 1-deoxy-D-xylulose 5-
CC phosphate biosynthesis. {ECO:0000305|PubMed:23042035}.
CC -!- DISRUPTION PHENOTYPE: Disruption of the gene abolishes the ability to
CC utilize 5'-methylthioadenosine (MTA) as a sole sulfur source
CC (PubMed:18826254). Mutant cannot release methanethiol upon MTA feeding
CC and accumulates MTRu-1P (PubMed:23042035). Inactivation of the gene
CC increases ethylene production from MTA-grown cells (PubMed:29133429).
CC {ECO:0000269|PubMed:18826254, ECO:0000269|PubMed:23042035,
CC ECO:0000269|PubMed:29133429}.
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type IV
CC subfamily. {ECO:0000305}.
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DR EMBL; CP000230; ABC22798.1; -; Genomic_DNA.
DR RefSeq; WP_011389751.1; NC_007643.1.
DR RefSeq; YP_427085.1; NC_007643.1.
DR AlphaFoldDB; Q2RSU7; -.
DR SMR; Q2RSU7; -.
DR IntAct; Q2RSU7; 1.
DR STRING; 269796.Rru_A1998; -.
DR EnsemblBacteria; ABC22798; ABC22798; Rru_A1998.
DR KEGG; rru:Rru_A1998; -.
DR PATRIC; fig|269796.9.peg.2083; -.
DR eggNOG; COG1850; Bacteria.
DR HOGENOM; CLU_031450_3_1_5; -.
DR OMA; IEQSVEC; -.
DR OrthoDB; 848380at2; -.
DR PhylomeDB; Q2RSU7; -.
DR BioCyc; MetaCyc:MON-17871; -.
DR BRENDA; 5.3.3.23; 5420.
DR UniPathway; UPA00064; -.
DR UniPathway; UPA00904; -.
DR Proteomes; UP000001929; Chromosome.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:InterPro.
DR GO; GO:0052865; P:1-deoxy-D-xylulose 5-phosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0015977; P:carbon fixation; IEA:InterPro.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.110; -; 1.
DR Gene3D; 3.30.70.150; -; 1.
DR InterPro; IPR033966; RuBisCO.
DR InterPro; IPR000685; RuBisCO_lsu_C.
DR InterPro; IPR036376; RuBisCO_lsu_C_sf.
DR InterPro; IPR036422; RuBisCO_lsu_N_sf.
DR PANTHER; PTHR42704; PTHR42704; 1.
DR Pfam; PF00016; RuBisCO_large; 1.
DR SUPFAM; SSF51649; SSF51649; 1.
DR SUPFAM; SSF54966; SSF54966; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Isomerase; Methionine biosynthesis;
KW Reference proteome.
FT CHAIN 1..374
FT /note="5-methylthioribulose-1-phosphate isomerase"
FT /id="PRO_0000445578"
SQ SEQUENCE 374 AA; 38880 MW; 304A089A23FCC187 CRC64;
MTDRLRATYR VKATAASIEA RAKGIAVEQS VEMPLSAIDD PAVLDGIVGV VEEITERGED
CFEVRLALST ATIGGDAGQL FNMLFGNTSL QDDTVLLDID LPDDLLASFG GPNIGAAGLR
ARVGASADRA LTCSALKPQG LPPDRLADLA RRMALGGLDF IKDDHGMADQ AYAPFASRVG
AVAAAVDEVN RQTGGQTRYL PSLSGHLDQL RSQVRTGLDH GIDTFLIAPM IVGPSTFHAV
VREFPGAAFF AHPTLAGPSR IAPPAHFGKL FRLLGADAVI FPNSGGRFGY SRDTCQAVAE
AALGPWGGLH ASLPVPAGGM SLARVPEMIA TYGPDVIVLI GGNLLEARDR LTEETAAFVA
SVAGAASRGC GLAP
