MTBC_PHYPA
ID MTBC_PHYPA Reviewed; 505 AA.
AC A9RBS1;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Probable bifunctional methylthioribulose-1-phosphate dehydratase/enolase-phosphatase E1 {ECO:0000255|HAMAP-Rule:MF_03118};
DE Includes:
DE RecName: Full=Methylthioribulose-1-phosphate dehydratase {ECO:0000255|HAMAP-Rule:MF_03118};
DE Short=MTRu-1-P dehydratase {ECO:0000255|HAMAP-Rule:MF_03118};
DE EC=4.2.1.109 {ECO:0000255|HAMAP-Rule:MF_03118};
DE Includes:
DE RecName: Full=Enolase-phosphatase E1 {ECO:0000255|HAMAP-Rule:MF_03118};
DE EC=3.1.3.77 {ECO:0000255|HAMAP-Rule:MF_03118};
DE AltName: Full=2,3-diketo-5-methylthio-1-phosphopentane phosphatase {ECO:0000255|HAMAP-Rule:MF_03118};
GN ORFNames=PHYPADRAFT_111231;
OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX NCBI_TaxID=3218;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004;
RX PubMed=18079367; DOI=10.1126/science.1150646;
RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA Boore J.L.;
RT "The Physcomitrella genome reveals evolutionary insights into the conquest
RT of land by plants.";
RL Science 319:64-69(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-methyl-5-thio-D-ribulose 1-phosphate = 5-methylsulfanyl-2,3-
CC dioxopentyl phosphate + H2O; Xref=Rhea:RHEA:15549, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:58548, ChEBI:CHEBI:58828; EC=4.2.1.109;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03118};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O = 1,2-
CC dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate;
CC Xref=Rhea:RHEA:21700, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:49252, ChEBI:CHEBI:58828; EC=3.1.3.77;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03118};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03118};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03118};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03118};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03118};
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 2/6. {ECO:0000255|HAMAP-Rule:MF_03118}.
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_03118}.
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 4/6. {ECO:0000255|HAMAP-Rule:MF_03118}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the aldolase class II
CC family. MtnB subfamily. {ECO:0000255|HAMAP-Rule:MF_03118}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the HAD-like
CC hydrolase superfamily. MasA/MtnC family. {ECO:0000255|HAMAP-
CC Rule:MF_03118}.
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DR EMBL; DS544890; EDQ83928.1; -; Genomic_DNA.
DR RefSeq; XP_001751611.1; XM_001751559.1.
DR AlphaFoldDB; A9RBS1; -.
DR SMR; A9RBS1; -.
DR STRING; 3218.PP1S1_661V6.3; -.
DR EnsemblPlants; Pp3c3_4430V3.1; Pp3c3_4430V3.1; Pp3c3_4430.
DR EnsemblPlants; Pp3c3_4430V3.2; Pp3c3_4430V3.2; Pp3c3_4430.
DR Gramene; Pp3c3_4430V3.1; Pp3c3_4430V3.1; Pp3c3_4430.
DR Gramene; Pp3c3_4430V3.2; Pp3c3_4430V3.2; Pp3c3_4430.
DR eggNOG; KOG2630; Eukaryota.
DR eggNOG; KOG2631; Eukaryota.
DR HOGENOM; CLU_023273_3_1_1; -.
DR InParanoid; A9RBS1; -.
DR OMA; RNNVGRH; -.
DR OrthoDB; 436252at2759; -.
DR UniPathway; UPA00904; UER00875.
DR UniPathway; UPA00904; UER00876.
DR UniPathway; UPA00904; UER00877.
DR Proteomes; UP000006727; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0043715; F:2,3-diketo-5-methylthiopentyl-1-phosphate enolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043716; F:2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043874; F:acireductone synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046570; F:methylthioribulose 1-phosphate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
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; cd01629; HAD_EP; 1.
DR Gene3D; 3.40.225.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR HAMAP; MF_03116; Salvage_MtnB_euk; 1.
DR HAMAP; MF_03118; Salvage_MtnBC; 1.
DR InterPro; IPR001303; Aldolase_II/adducin_N.
DR InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR InterPro; IPR023943; Enolase-ppase_E1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR017714; MethylthioRu-1-P_deHdtase_MtnB.
DR InterPro; IPR027505; MtnB_viridiplantae.
DR InterPro; IPR027514; Salvage_MtnB_euk.
DR PANTHER; PTHR10640; PTHR10640; 1.
DR Pfam; PF00596; Aldolase_II; 1.
DR SFLD; SFLDF00044; enolase-phosphatase; 1.
DR SMART; SM01007; Aldolase_II; 1.
DR SUPFAM; SSF53639; SSF53639; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01691; enolase-ppase; 1.
DR TIGRFAMs; TIGR03328; salvage_mtnB; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Hydrolase; Lyase; Magnesium; Metal-binding;
KW Methionine biosynthesis; Multifunctional enzyme; Reference proteome; Zinc.
FT CHAIN 1..505
FT /note="Probable bifunctional methylthioribulose-1-phosphate
FT dehydratase/enolase-phosphatase E1"
FT /id="PRO_0000394159"
FT REGION 1..237
FT /note="Methylthioribulose-1-phosphate dehydratase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT REGION 266..505
FT /note="Enolase-phosphatase E1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT ACT_SITE 152
FT /note="Proton donor/acceptor; for methylthioribulose-1-
FT phosphate dehydratase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT BINDING 109
FT /ligand="substrate"
FT /ligand_label="1"
FT /ligand_note="for methylthioribulose-1-phosphate
FT dehydratase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT BINDING 202
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT BINDING 269
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT BINDING 271
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT BINDING 404..405
FT /ligand="substrate"
FT /ligand_label="2"
FT /ligand_note="for enolase-phosphatase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT BINDING 438
FT /ligand="substrate"
FT /ligand_label="2"
FT /ligand_note="for enolase-phosphatase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT BINDING 464
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
SQ SEQUENCE 505 AA; 55425 MW; D5E680CDF5BD8907 CRC64;
MGLDKDGISN IAKERIASSL VEDTKDLAAE LCKHFYNQGW VSGTGGSITL KVLESDVDVQ
ERLIVMAPSG VQKERMLPVD MYVLSSDGTV LSAPPAKGAP HKPPKCSECC PLFLKAYKMR
NAGAVIHSHG LESCLATMIN PTAKEFRITH MEMIKGIAGH GYYDELVVPI IENSAREYEL
TDALAAAMEA YPKATAVLVR NHGIYIWGDS WISAKTQAEC YHYLFNAALK LHQLGLDPAD
AKHGPLTRPQ TLPDFANKRA TSKNVFVLDI EGTTTPISFV TEVLFPYARE NVSSFFKSTY
NSPETLNDIR LLRDQVHEDL RNNVPGATEI PVESAGIDAV VAAIEKNVQA MIKADRKVTA
LKELQGHIWR IGYENGELKG SVFEDVPEAL AKWDARGIKT YIYSSGSREA QKLIFGNTNF
GDLRVYLSGF FDTTIGHKRE ARSYKEIFLT LGVDHPSCIT FATDVLAEAV AAKEAGLQAV
LLLRPGNAPL PSDHGFRTAK SLLEL
