LERI_MYCS2
ID LERI_MYCS2 Reviewed; 263 AA.
AC A0R756; I7GGP3;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=L-erythrulose-1-phosphate isomerase {ECO:0000305|PubMed:26978037};
DE EC=5.3.1.33 {ECO:0000269|PubMed:26560079, ECO:0000305|PubMed:26978037};
GN Name=lerI {ECO:0000303|PubMed:26560079};
GN Synonyms=tpiA {ECO:0000312|EMBL:ABK75255.1};
GN OrderedLocusNames=MSMEG_6785 {ECO:0000312|EMBL:ABK75255.1},
GN MSMEI_6603 {ECO:0000312|EMBL:AFP43029.1};
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND PATHWAY.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=26560079; DOI=10.1021/jacs.5b08968;
RA Huang H., Carter M.S., Vetting M.W., Al-Obaidi N., Patskovsky Y.,
RA Almo S.C., Gerlt J.A.;
RT "A general strategy for the discovery of metabolic pathways: D-threitol, L-
RT threitol, and erythritol utilization in Mycobacterium smegmatis.";
RL J. Am. Chem. Soc. 137:14570-14573(2015).
RN [5]
RP ERRATUM OF PUBMED:26560079, AND CORRECTION TO SUBSTRATE IDENTIFICATION.
RX PubMed=26978037; DOI=10.1021/jacs.6b01906;
RA Huang H., Carter M.S., Vetting M.W., Al-Obaidi N., Patskovsky Y.,
RA Almo S.C., Gerlt J.A.;
RT "Correction to 'A general strategy for the discovery of metabolic pathways:
RT D-threitol, L-threitol, and erythritol utilization in Mycobacterium
RT smegmatis'.";
RL J. Am. Chem. Soc. 138:4267-4267(2016).
CC -!- FUNCTION: Catalyzes the isomerization of L-erythrulose-1P to D-
CC erythrulose-4P. Involved in the degradation pathway of L-threitol, that
CC allows M.smegmatis to grow on this compound as the sole carbon source.
CC {ECO:0000269|PubMed:26560079, ECO:0000305|PubMed:26978037}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-erythrulose 1-phosphate = D-erythrulose 4-phosphate;
CC Xref=Rhea:RHEA:49588, ChEBI:CHEBI:58002, ChEBI:CHEBI:90796;
CC EC=5.3.1.33; Evidence={ECO:0000269|PubMed:26560079,
CC ECO:0000305|PubMed:26978037};
CC -!- PATHWAY: Carbohydrate metabolism; L-threitol degradation.
CC {ECO:0000269|PubMed:26560079}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are totally unable to
CC grow on L-threitol. {ECO:0000269|PubMed:26560079}.
CC -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC {ECO:0000305}.
CC -!- CAUTION: The substrate of the reaction was originally identified as L-
CC erythrulose 4-phosphate (PubMed:26560079). It was then corrected to L-
CC erythrulose 1-phosphate by the same group (PubMed:26978037).
CC {ECO:0000269|PubMed:26560079, ECO:0000269|PubMed:26978037}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AFP43029.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000480; ABK75255.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP43029.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011731538.1; NZ_SIJM01000001.1.
DR RefSeq; YP_890994.1; NC_008596.1.
DR AlphaFoldDB; A0R756; -.
DR SMR; A0R756; -.
DR STRING; 246196.MSMEI_6603; -.
DR EnsemblBacteria; ABK75255; ABK75255; MSMEG_6785.
DR EnsemblBacteria; AFP43029; AFP43029; MSMEI_6603.
DR GeneID; 66738043; -.
DR KEGG; msg:MSMEI_6603; -.
DR KEGG; msm:MSMEG_6785; -.
DR PATRIC; fig|246196.19.peg.6606; -.
DR eggNOG; COG0149; Bacteria.
DR OMA; CIGEKTH; -.
DR OrthoDB; 1266295at2; -.
DR BioCyc; MetaCyc:MON-19894; -.
DR UniPathway; UPA01067; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0016857; F:racemase and epimerase activity, acting on carbohydrates and derivatives; IDA:UniProtKB.
DR GO; GO:0004807; F:triose-phosphate isomerase activity; IEA:InterPro.
DR GO; GO:0016052; P:carbohydrate catabolic process; IMP:UniProtKB.
DR GO; GO:0009758; P:carbohydrate utilization; IMP:UniProtKB.
DR CDD; cd00311; TIM; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR035990; TIM_sf.
DR InterPro; IPR000652; Triosephosphate_isomerase.
DR InterPro; IPR020861; Triosephosphate_isomerase_AS.
DR PANTHER; PTHR21139; PTHR21139; 1.
DR Pfam; PF00121; TIM; 1.
DR SUPFAM; SSF51351; SSF51351; 1.
DR PROSITE; PS00171; TIM_1; 1.
DR PROSITE; PS51440; TIM_2; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Isomerase; Reference proteome.
FT CHAIN 1..263
FT /note="L-erythrulose-1-phosphate isomerase"
FT /id="PRO_0000435519"
FT ACT_SITE 106
FT /note="Electrophile"
FT /evidence="ECO:0000250|UniProtKB:P9WG43"
FT ACT_SITE 178
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P9WG43"
SQ SEQUENCE 263 AA; 28295 MW; 966EA3BC94FC6BF8 CRC64;
MPDARALGAA QLWIGTSWKM NKGLAESRGY ARELAEYVAA KPPAGVQPFI IPSFTALTTV
RDALGDDSPV LLGVQNAHWE DHGAWTGEVS VAQAKDAGAQ IVEIGHSERR EHFGETVETT
RLKVAAALHH GLVPLLCIGE SAENKQAGES SRFILEQAAG ALEGLTDEHL ARVLIAYEPI
WAIGENGRPA TVEELRQPFD DLAREYGCRT MGLLYGGSVN TDNAEDLLGI DHVTGLFIGR
AAWQLPGYVR ILEMAAAHPK AKA
