DERI1_MYCS2
ID DERI1_MYCS2 Reviewed; 153 AA.
AC A0QXE5;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=D-erythrulose-4-phosphate isomerase 1 {ECO:0000303|PubMed:26560079};
DE EC=5.3.1.34 {ECO:0000269|PubMed:26560079};
GN Name=derI1 {ECO:0000303|PubMed:26560079};
GN OrderedLocusNames=MSMEG_3272 {ECO:0000312|EMBL:ABK70126.1},
GN MSMEI_3188 {ECO:0000312|EMBL:AFP39651.1};
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, INDUCTION, 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).
CC -!- FUNCTION: Catalyzes the isomerization of D-erythrulose-4P to D-
CC erythrose-4P. Involved in the degradation pathways of erythritol and D-
CC threitol, that allow M.smegmatis to grow on these compounds as the sole
CC carbon source. {ECO:0000269|PubMed:26560079}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-erythrulose 4-phosphate = D-erythrose 4-phosphate;
CC Xref=Rhea:RHEA:48784, ChEBI:CHEBI:16897, ChEBI:CHEBI:90796;
CC EC=5.3.1.34; Evidence={ECO:0000269|PubMed:26560079};
CC -!- PATHWAY: Carbohydrate metabolism; erythritol degradation.
CC {ECO:0000269|PubMed:26560079}.
CC -!- PATHWAY: Carbohydrate metabolism; D-threitol degradation.
CC {ECO:0000269|PubMed:26560079}.
CC -!- INDUCTION: Up-regulated during growth on erythritol, D-threitol or L-
CC threitol relative to growth on glycerol. {ECO:0000269|PubMed:26560079}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking both derI1 and derI2 are totally
CC unable to grow on D-threitol or on erythritol.
CC {ECO:0000269|PubMed:26560079}.
CC -!- SIMILARITY: Belongs to the LacAB/RpiB family. {ECO:0000305}.
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DR EMBL; CP000480; ABK70126.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP39651.1; -; Genomic_DNA.
DR RefSeq; WP_011728942.1; NZ_SIJM01000015.1.
DR RefSeq; YP_887583.1; NC_008596.1.
DR AlphaFoldDB; A0QXE5; -.
DR SMR; A0QXE5; -.
DR STRING; 246196.MSMEI_3188; -.
DR EnsemblBacteria; ABK70126; ABK70126; MSMEG_3272.
DR EnsemblBacteria; AFP39651; AFP39651; MSMEI_3188.
DR GeneID; 66734672; -.
DR KEGG; msg:MSMEI_3188; -.
DR KEGG; msm:MSMEG_3272; -.
DR PATRIC; fig|246196.19.peg.3233; -.
DR eggNOG; COG0698; Bacteria.
DR OMA; ETHHANQ; -.
DR OrthoDB; 1346802at2; -.
DR BioCyc; MetaCyc:MON-19891; -.
DR UniPathway; UPA01065; -.
DR UniPathway; UPA01066; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0016861; F:intramolecular oxidoreductase activity, interconverting aldoses and ketoses; IDA:UniProtKB.
DR GO; GO:0016052; P:carbohydrate catabolic process; IMP:UniProtKB.
DR GO; GO:0009758; P:carbohydrate utilization; IMP:UniProtKB.
DR GO; GO:0071322; P:cellular response to carbohydrate stimulus; IDA:UniProtKB.
DR Gene3D; 3.40.1400.10; -; 1.
DR InterPro; IPR011860; Rib-5-P_Isoase_Actino.
DR InterPro; IPR003500; RpiB_LacA_LacB.
DR InterPro; IPR036569; RpiB_LacA_LacB_sf.
DR Pfam; PF02502; LacAB_rpiB; 1.
DR PIRSF; PIRSF005384; RpiB_LacA_B; 1.
DR SUPFAM; SSF89623; SSF89623; 1.
DR TIGRFAMs; TIGR02133; RPI_actino; 1.
DR TIGRFAMs; TIGR00689; rpiB_lacA_lacB; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Isomerase; Reference proteome.
FT CHAIN 1..153
FT /note="D-erythrulose-4-phosphate isomerase 1"
FT /id="PRO_0000435517"
FT ACT_SITE 69
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P37351"
SQ SEQUENCE 153 AA; 16108 MW; 5BBD3ED333690C35 CRC64;
MALRVVVGAD DAGYEYKEAL KGDLAADDRV TEVIDVGVGA DEDTAYPHVA VAAARLIAEG
KADRALLVCG TGLGVAISAN KVPGIRAVTA HDSFSVERSV LSNNAQVLCF GQRVVGLELA
RRLAREWLGY EFDPTSKSAE KVQAICGYEP ATS
