MTNW_BACSU
ID MTNW_BACSU Reviewed; 405 AA.
AC O31666;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=2,3-diketo-5-methylthiopentyl-1-phosphate enolase;
DE Short=DK-MTP-1-P enolase;
DE EC=5.3.2.5;
DE AltName: Full=RuBisCO-like protein;
DE Short=RLP;
GN Name=mtnW; Synonyms=ykrW; OrderedLocusNames=BSU13590;
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).
CC -!- FUNCTION: Catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-
CC phosphate (DK-MTP-1-P) into 2-hydroxy-3-keto-5-methylthiopentenyl-1-
CC phosphate (HK-MTPenyl-1-P). {ECO:0000269|PubMed:14551435}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-methylsulfanyl-2,3-dioxopentyl phosphate = 2-hydroxy-5-
CC methylsulfanyl-3-oxopent-1-enyl phosphate; Xref=Rhea:RHEA:18769,
CC ChEBI:CHEBI:58828, ChEBI:CHEBI:59505; EC=5.3.2.5;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000305};
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 3/6.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- MISCELLANEOUS: Has no RuBP-carboxylation activity.
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type IV
CC subfamily. {ECO:0000305}.
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DR EMBL; AL009126; CAB13232.2; -; Genomic_DNA.
DR PIR; G69863; G69863.
DR RefSeq; NP_389242.1; NC_000964.3.
DR RefSeq; WP_003245108.1; NZ_JNCM01000035.1.
DR PDB; 2ZVI; X-ray; 2.30 A; A/B/C/D=1-405.
DR PDBsum; 2ZVI; -.
DR AlphaFoldDB; O31666; -.
DR SMR; O31666; -.
DR IntAct; O31666; 1.
DR MINT; O31666; -.
DR STRING; 224308.BSU13590; -.
DR PaxDb; O31666; -.
DR PRIDE; O31666; -.
DR EnsemblBacteria; CAB13232; CAB13232; BSU_13590.
DR GeneID; 939339; -.
DR KEGG; bsu:BSU13590; -.
DR PATRIC; fig|224308.179.peg.1476; -.
DR eggNOG; COG1850; Bacteria.
DR InParanoid; O31666; -.
DR OMA; IHGHPDG; -.
DR BioCyc; BSUB:BSU13590-MON; -.
DR BioCyc; MetaCyc:BSU13590-MON; -.
DR UniPathway; UPA00904; UER00876.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0043715; F:2,3-diketo-5-methylthiopentyl-1-phosphate enolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:InterPro.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniPathway.
DR GO; GO:0019284; P:L-methionine salvage from S-adenosylmethionine; IEA:UniProtKB-UniRule.
DR CDD; cd08209; RLP_DK-MTP-1-P-enolase; 1.
DR Gene3D; 3.20.20.110; -; 1.
DR Gene3D; 3.30.70.150; -; 1.
DR HAMAP; MF_01679; Salvage_MtnW; 1.
DR InterPro; IPR017717; Diketo-Methiopentyl-P_enolase.
DR InterPro; IPR033966; RuBisCO.
DR InterPro; IPR000685; RuBisCO_lsu_C.
DR InterPro; IPR036376; RuBisCO_lsu_C_sf.
DR InterPro; IPR017443; RuBisCO_lsu_fd_N.
DR InterPro; IPR036422; RuBisCO_lsu_N_sf.
DR PANTHER; PTHR42704; PTHR42704; 1.
DR Pfam; PF00016; RuBisCO_large; 2.
DR Pfam; PF02788; RuBisCO_large_N; 1.
DR SFLD; SFLDF00157; 2_3-diketo-5-methylthiopentyl; 1.
DR SUPFAM; SSF51649; SSF51649; 1.
DR SUPFAM; SSF54966; SSF54966; 1.
DR TIGRFAMs; TIGR03332; salvage_mtnW; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Isomerase; Magnesium; Metal-binding;
KW Methionine biosynthesis; Reference proteome.
FT CHAIN 1..405
FT /note="2,3-diketo-5-methylthiopentyl-1-phosphate enolase"
FT /id="PRO_0000062692"
FT ACT_SITE 92
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 167..170
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 258
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 330
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 352..353
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 167
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000250"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:2ZVI"
FT HELIX 17..27
FT /evidence="ECO:0007829|PDB:2ZVI"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:2ZVI"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:2ZVI"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:2ZVI"
FT STRAND 50..55
FT /evidence="ECO:0007829|PDB:2ZVI"
FT STRAND 67..74
FT /evidence="ECO:0007829|PDB:2ZVI"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:2ZVI"
FT HELIX 82..90
FT /evidence="ECO:0007829|PDB:2ZVI"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:2ZVI"
FT STRAND 96..105
FT /evidence="ECO:0007829|PDB:2ZVI"
FT HELIX 108..112
FT /evidence="ECO:0007829|PDB:2ZVI"
FT HELIX 120..128
FT /evidence="ECO:0007829|PDB:2ZVI"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:2ZVI"
FT HELIX 148..160
FT /evidence="ECO:0007829|PDB:2ZVI"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:2ZVI"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:2ZVI"
FT HELIX 180..198
FT /evidence="ECO:0007829|PDB:2ZVI"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:2ZVI"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:2ZVI"
FT HELIX 215..224
FT /evidence="ECO:0007829|PDB:2ZVI"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:2ZVI"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:2ZVI"
FT HELIX 239..247
FT /evidence="ECO:0007829|PDB:2ZVI"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:2ZVI"
FT HELIX 262..265
FT /evidence="ECO:0007829|PDB:2ZVI"
FT STRAND 269..273
FT /evidence="ECO:0007829|PDB:2ZVI"
FT HELIX 275..278
FT /evidence="ECO:0007829|PDB:2ZVI"
FT HELIX 281..285
FT /evidence="ECO:0007829|PDB:2ZVI"
FT STRAND 289..293
FT /evidence="ECO:0007829|PDB:2ZVI"
FT STRAND 296..300
FT /evidence="ECO:0007829|PDB:2ZVI"
FT HELIX 304..315
FT /evidence="ECO:0007829|PDB:2ZVI"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:2ZVI"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:2ZVI"
FT HELIX 336..343
FT /evidence="ECO:0007829|PDB:2ZVI"
FT STRAND 346..350
FT /evidence="ECO:0007829|PDB:2ZVI"
FT HELIX 352..357
FT /evidence="ECO:0007829|PDB:2ZVI"
FT HELIX 361..377
FT /evidence="ECO:0007829|PDB:2ZVI"
FT HELIX 382..388
FT /evidence="ECO:0007829|PDB:2ZVI"
FT HELIX 390..399
FT /evidence="ECO:0007829|PDB:2ZVI"
SQ SEQUENCE 405 AA; 44043 MW; 7680666C6D1E9EA3 CRC64;
MSELLATYLL TEPGADTEKK AEQIATGLTV GSWTDLPLVK QEQMQKHKGR VIKVEEREGT
AASEKQAVIT IAYPEINFSQ DIPALLTTVF GKLSLDGKIK LIDLHFSEAF KRALPGPKFG
VYGIRKLLGE FERPLLMSIF KGVIGRDLSD IKEQLRQQAL GGVDLIKDDE IFFETGLAPF
ETRIAEGKQI LKETYEQTGH KTLYAVNLTG RTADLKDKAR RAAELGADAL LFNVFAYGLD
VMQGLAEDPE IPVPIMAHPA VSGAFTSSPF YGFSHALLLG KLNRYCGADF SLFPSPYGSV
ALPRADALAI HEECVREDAF NQTFAVPSAG IHPGMVPLLM RDFGIDHIIN AGGGVHGHPN
GAQGGGRAFR AIIDAVLEAQ PIDEKAEQCK DLKLALDKWG KAEAV
