MTNA_BACSU
ID MTNA_BACSU Reviewed; 353 AA.
AC O31662;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Methylthioribose-1-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_01678};
DE Short=M1Pi {ECO:0000255|HAMAP-Rule:MF_01678};
DE Short=MTR-1-P isomerase {ECO:0000255|HAMAP-Rule:MF_01678};
DE EC=5.3.1.23 {ECO:0000255|HAMAP-Rule:MF_01678};
DE AltName: Full=S-methyl-5-thioribose-1-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_01678};
GN Name=mtnA {ECO:0000255|HAMAP-Rule:MF_01678}; Synonyms=ykrS;
GN OrderedLocusNames=BSU13550;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP REVIEW.
RX PubMed=12022921; DOI=10.1186/1471-2180-2-8;
RA Sekowska A., Danchin A.;
RT "The methionine salvage pathway in Bacillus subtilis.";
RL BMC Microbiol. 2:8-8(2002).
RN [3]
RP FUNCTION.
RX PubMed=14551435; DOI=10.1126/science.1086997;
RA Ashida H., Saito Y., Kojima C., Kobayashi K., Ogasawara N., Yokota A.;
RT "A functional link between RuBisCO-like protein of Bacillus and
RT photosynthetic RuBisCO.";
RL Science 302:286-290(2003).
RN [4]
RP NOMENCLATURE.
RX PubMed=15102328; DOI=10.1186/1471-2180-4-9;
RA Sekowska A., Denervaud V., Ashida H., Michoud K., Haas D., Yokota A.,
RA Danchin A.;
RT "Bacterial variations on the methionine salvage pathway.";
RL BMC Microbiol. 4:9-9(2004).
RN [5]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=17690466; DOI=10.1271/bbb.70209;
RA Saito Y., Ashida H., Kojima C., Tamura H., Matsumura H., Kai Y., Yokota A.;
RT "Enzymatic characterization of 5-methylthioribose 1-phosphate isomerase
RT from Bacillus subtilis.";
RL Biosci. Biotechnol. Biochem. 71:2021-2028(2007).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH SULFATE IONS AND
RP 5-METHYLTHIORIBULOSE 1-PHOSPHATE, AND SUBUNIT.
RX PubMed=18156470; DOI=10.1110/ps.073169008;
RA Tamura H., Saito Y., Ashida H., Inoue T., Kai Y., Yokota A., Matsumura H.;
RT "Crystal structure of 5-methylthioribose 1-phosphate isomerase product
RT complex from Bacillus subtilis: implications for catalytic mechanism.";
RL Protein Sci. 17:126-135(2008).
CC -!- FUNCTION: Catalyzes the interconversion of methylthioribose-1-phosphate
CC (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
CC {ECO:0000255|HAMAP-Rule:MF_01678, ECO:0000269|PubMed:14551435}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-
CC D-ribulose 1-phosphate; Xref=Rhea:RHEA:19989, ChEBI:CHEBI:58533,
CC ChEBI:CHEBI:58548; EC=5.3.1.23; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01678};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=138 uM for methylthioribose-1-phosphate (at pH 8.5 and 35 degrees
CC Celsius) {ECO:0000269|PubMed:17690466};
CC Vmax=20.4 umol/min/mg enzyme (at pH 8.5 and 35 degrees Celsius)
CC {ECO:0000269|PubMed:17690466};
CC pH dependence:
CC Optimum pH is 8.1. {ECO:0000269|PubMed:17690466};
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius.
CC {ECO:0000269|PubMed:17690466};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage
CC pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate:
CC step 1/6. {ECO:0000255|HAMAP-Rule:MF_01678}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01678,
CC ECO:0000269|PubMed:17690466, ECO:0000269|PubMed:18156470}.
CC -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family.
CC MtnA subfamily. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a translation initiation factor.
CC {ECO:0000305}.
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DR EMBL; AL009126; CAB13228.1; -; Genomic_DNA.
DR PIR; C69863; C69863.
DR RefSeq; NP_389238.1; NC_000964.3.
DR RefSeq; WP_003232498.1; NZ_JNCM01000035.1.
DR PDB; 2YRF; X-ray; 2.70 A; A/B=1-353.
DR PDB; 2YVK; X-ray; 2.40 A; A/B/C/D=1-353.
DR PDBsum; 2YRF; -.
DR PDBsum; 2YVK; -.
DR AlphaFoldDB; O31662; -.
DR SMR; O31662; -.
DR IntAct; O31662; 1.
DR MINT; O31662; -.
DR STRING; 224308.BSU13550; -.
DR PaxDb; O31662; -.
DR PRIDE; O31662; -.
DR EnsemblBacteria; CAB13228; CAB13228; BSU_13550.
DR GeneID; 939341; -.
DR KEGG; bsu:BSU13550; -.
DR PATRIC; fig|224308.179.peg.1472; -.
DR eggNOG; COG0182; Bacteria.
DR InParanoid; O31662; -.
DR OMA; GDVIMTH; -.
DR PhylomeDB; O31662; -.
DR BioCyc; BSUB:BSU13550-MON; -.
DR BRENDA; 5.3.1.23; 658.
DR UniPathway; UPA00904; UER00874.
DR EvolutionaryTrace; O31662; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0046523; F:S-methyl-5-thioribose-1-phosphate isomerase activity; IBA:GO_Central.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IBA:GO_Central.
DR GO; GO:0019284; P:L-methionine salvage from S-adenosylmethionine; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.120.420; -; 1.
DR Gene3D; 3.40.50.10470; -; 1.
DR HAMAP; MF_01678; Salvage_MtnA; 1.
DR InterPro; IPR000649; IF-2B-related.
DR InterPro; IPR005251; IF-M1Pi.
DR InterPro; IPR042529; IF_2B-like_C.
DR InterPro; IPR011559; Initiation_fac_2B_a/b/d.
DR InterPro; IPR027363; M1Pi_N.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR Pfam; PF01008; IF-2B; 1.
DR SUPFAM; SSF100950; SSF100950; 1.
DR TIGRFAMs; TIGR00524; eIF-2B_rel; 1.
DR TIGRFAMs; TIGR00512; salvage_mtnA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Isomerase; Methionine biosynthesis;
KW Reference proteome.
FT CHAIN 1..353
FT /note="Methylthioribose-1-phosphate isomerase"
FT /id="PRO_0000156092"
FT ACT_SITE 240
FT /note="Proton donor"
FT BINDING 51..53
FT /ligand="substrate"
FT BINDING 94
FT /ligand="substrate"
FT BINDING 199
FT /ligand="substrate"
FT BINDING 250..251
FT /ligand="substrate"
FT SITE 160
FT /note="Transition state stabilizer"
FT HELIX 2..6
FT /evidence="ECO:0007829|PDB:2YVK"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:2YVK"
FT STRAND 18..21
FT /evidence="ECO:0007829|PDB:2YVK"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:2YVK"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:2YVK"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:2YVK"
FT HELIX 38..46
FT /evidence="ECO:0007829|PDB:2YVK"
FT HELIX 53..68
FT /evidence="ECO:0007829|PDB:2YVK"
FT HELIX 76..91
FT /evidence="ECO:0007829|PDB:2YVK"
FT HELIX 98..110
FT /evidence="ECO:0007829|PDB:2YVK"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:2YVK"
FT HELIX 117..146
FT /evidence="ECO:0007829|PDB:2YVK"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:2YVK"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:2YVK"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:2YVK"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:2YVK"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:2YRF"
FT HELIX 175..182
FT /evidence="ECO:0007829|PDB:2YVK"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:2YVK"
FT TURN 195..198
FT /evidence="ECO:0007829|PDB:2YVK"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:2YVK"
FT HELIX 204..209
FT /evidence="ECO:0007829|PDB:2YVK"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:2YVK"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:2YVK"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:2YVK"
FT HELIX 223..229
FT /evidence="ECO:0007829|PDB:2YVK"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:2YVK"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:2YVK"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:2YVK"
FT HELIX 254..263
FT /evidence="ECO:0007829|PDB:2YVK"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:2YVK"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:2YVK"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:2YVK"
FT HELIX 295..298
FT /evidence="ECO:0007829|PDB:2YVK"
FT STRAND 315..320
FT /evidence="ECO:0007829|PDB:2YVK"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:2YVK"
FT STRAND 326..330
FT /evidence="ECO:0007829|PDB:2YVK"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:2YVK"
FT HELIX 339..346
FT /evidence="ECO:0007829|PDB:2YVK"
SQ SEQUENCE 353 AA; 38860 MW; D8866535BE127DC6 CRC64;
MTHSFAVPRS VEWKETAITI LNQQKLPDET EYLELTTKED VFDAIVTLKV RGAPAIGITA
AFGLALAAKD IETDNVTEFR RRLEDIKQYL NSSRPTAINL SWALERLSHS VENAISVNEA
KTNLVHEAIQ IQVEDEETCR LIGQNALQLF KKGDRIMTIC NAGSIATSRY GTALAPFYLA
KQKDLGLHIY ACETRPVLQG SRLTAWELMQ GGIDVTLITD SMAAHTMKEK QISAVIVGAD
RIAKNGDTAN KIGTYGLAIL ANAFDIPFFV AAPLSTFDTK VKCGADIPIE ERDPEEVRQI
SGVRTAPSNV PVFNPAFDIT PHDLISGIIT EKGIMTGNYE EEIEQLFKGE KVH
