MTNW_BACCR
ID MTNW_BACCR Reviewed; 414 AA.
AC Q819E8;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=2,3-diketo-5-methylthiopentyl-1-phosphate enolase {ECO:0000255|HAMAP-Rule:MF_01679};
DE Short=DK-MTP-1-P enolase {ECO:0000255|HAMAP-Rule:MF_01679};
DE EC=5.3.2.5 {ECO:0000255|HAMAP-Rule:MF_01679};
DE AltName: Full=RuBisCO-like protein {ECO:0000255|HAMAP-Rule:MF_01679};
DE Short=RLP {ECO:0000255|HAMAP-Rule:MF_01679};
GN Name=mtnW {ECO:0000255|HAMAP-Rule:MF_01679}; OrderedLocusNames=BC_4036;
OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC / NCTC 2599 / NRRL B-3711;
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT anthracis.";
RL Nature 423:87-91(2003).
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:0000255|HAMAP-Rule:MF_01679}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_01679};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01679};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01679};
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. {ECO:0000255|HAMAP-Rule:MF_01679}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01679}.
CC -!- MISCELLANEOUS: Has no RuBP-carboxylation activity. {ECO:0000255|HAMAP-
CC Rule:MF_01679}.
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type IV
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01679}.
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DR EMBL; AE016877; AAP10955.1; -; Genomic_DNA.
DR RefSeq; NP_833754.1; NC_004722.1.
DR RefSeq; WP_000014181.1; NZ_CP034551.1.
DR PDB; 3FK4; X-ray; 2.00 A; A/B=1-414.
DR PDBsum; 3FK4; -.
DR AlphaFoldDB; Q819E8; -.
DR SMR; Q819E8; -.
DR STRING; 226900.BC_4036; -.
DR EnsemblBacteria; AAP10955; AAP10955; BC_4036.
DR KEGG; bce:BC4036; -.
DR PATRIC; fig|226900.8.peg.4167; -.
DR HOGENOM; CLU_031450_3_1_9; -.
DR OMA; IHGHPDG; -.
DR UniPathway; UPA00904; UER00876.
DR EvolutionaryTrace; Q819E8; -.
DR Proteomes; UP000001417; 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:0015977; P:carbon fixation; 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; 1.
DR Pfam; PF02788; RuBisCO_large_N; 1.
DR SFLD; SFLDF00157; 2_3-diketo-5-methylthiopentyl; 1.
DR SFLD; SFLDS00014; RuBisCO; 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..414
FT /note="2,3-diketo-5-methylthiopentyl-1-phosphate enolase"
FT /id="PRO_0000062689"
FT ACT_SITE 99
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT BINDING 174..177
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT BINDING 174
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT BINDING 176
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT BINDING 177
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT BINDING 265
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT BINDING 338
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT BINDING 360..361
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT MOD_RES 174
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01679"
FT STRAND 4..12
FT /evidence="ECO:0007829|PDB:3FK4"
FT HELIX 17..27
FT /evidence="ECO:0007829|PDB:3FK4"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:3FK4"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:3FK4"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:3FK4"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:3FK4"
FT HELIX 61..67
FT /evidence="ECO:0007829|PDB:3FK4"
FT STRAND 72..80
FT /evidence="ECO:0007829|PDB:3FK4"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:3FK4"
FT HELIX 89..97
FT /evidence="ECO:0007829|PDB:3FK4"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:3FK4"
FT STRAND 103..113
FT /evidence="ECO:0007829|PDB:3FK4"
FT HELIX 115..118
FT /evidence="ECO:0007829|PDB:3FK4"
FT HELIX 127..135
FT /evidence="ECO:0007829|PDB:3FK4"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:3FK4"
FT HELIX 155..167
FT /evidence="ECO:0007829|PDB:3FK4"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:3FK4"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:3FK4"
FT HELIX 187..205
FT /evidence="ECO:0007829|PDB:3FK4"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:3FK4"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:3FK4"
FT HELIX 222..232
FT /evidence="ECO:0007829|PDB:3FK4"
FT STRAND 235..239
FT /evidence="ECO:0007829|PDB:3FK4"
FT HELIX 241..244
FT /evidence="ECO:0007829|PDB:3FK4"
FT HELIX 246..254
FT /evidence="ECO:0007829|PDB:3FK4"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:3FK4"
FT TURN 267..269
FT /evidence="ECO:0007829|PDB:3FK4"
FT HELIX 270..273
FT /evidence="ECO:0007829|PDB:3FK4"
FT STRAND 276..280
FT /evidence="ECO:0007829|PDB:3FK4"
FT HELIX 282..286
FT /evidence="ECO:0007829|PDB:3FK4"
FT HELIX 288..293
FT /evidence="ECO:0007829|PDB:3FK4"
FT STRAND 296..301
FT /evidence="ECO:0007829|PDB:3FK4"
FT HELIX 312..322
FT /evidence="ECO:0007829|PDB:3FK4"
FT STRAND 332..338
FT /evidence="ECO:0007829|PDB:3FK4"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:3FK4"
FT HELIX 344..351
FT /evidence="ECO:0007829|PDB:3FK4"
FT STRAND 353..358
FT /evidence="ECO:0007829|PDB:3FK4"
FT HELIX 360..365
FT /evidence="ECO:0007829|PDB:3FK4"
FT HELIX 369..385
FT /evidence="ECO:0007829|PDB:3FK4"
FT HELIX 396..404
FT /evidence="ECO:0007829|PDB:3FK4"
SQ SEQUENCE 414 AA; 45463 MW; AF43EE23B14D1EFB CRC64;
MSGIIATYLI HDDSHNLEKK AEQIALGLTI GSWTHLPHLL QEQLKQHKGN VIHVEELAEH
EHTNSYLRKK VKRGIIKIEY PLLNFSPDLP AILTTTFGKL SLDGEVKLID LTFSDELKKH
FPGPKFGIDG IRNLLQVHDR PLLMSIFKGM IGRNIGYLKT QLRDQAIGGV DIVKDDEILF
ENALTPLTKR IVSGKEVLQS VYETYGHKTL YAVNLTGRTF DLKENAKRAV QAGADILLFN
VFAYGLDVLQ SLAEDDEIPV PIMAHPAVSG AYSASKLYGV SSPLLLGKLL RYAGADFSLF
PSPYGSVALE KEEALAISKY LTEDDASFKK SFSVPSAGIH PGFVPFIVRD FGKDVVINAG
GGIHGHPNGA QGGGKAFRTA IDATLQNKPL HEVDDINLHS ALQIWGNPSY EVKL
