(data stored in ACNUC29543 zone)

SWISSPROT: A5GR43_SYNR3

ID   A5GR43_SYNR3            Unreviewed;       226 AA.
AC   A5GR43;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   08-MAY-2019, entry version 77.
DE   RecName: Full=Methylthioribulose-1-phosphate dehydratase {ECO:0000256|HAMAP-Rule:MF_01677};
DE            Short=MTRu-1-P dehydratase {ECO:0000256|HAMAP-Rule:MF_01677};
DE            EC=4.2.1.109 {ECO:0000256|HAMAP-Rule:MF_01677};
GN   Name=mtnB {ECO:0000256|HAMAP-Rule:MF_01677};
GN   OrderedLocusNames=SynRCC307_0449 {ECO:0000313|EMBL:CAK27352.1};
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278 {ECO:0000313|EMBL:CAK27352.1, ECO:0000313|Proteomes:UP000001115};
RN   [1] {ECO:0000313|Proteomes:UP000001115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307 {ECO:0000313|Proteomes:UP000001115};
RG   Genoscope;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the dehydration of methylthioribulose-1-
CC       phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-
CC       phosphate (DK-MTP-1-P). {ECO:0000256|HAMAP-Rule:MF_01677}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-methylsulfanyl-D-ribulose 1-phosphate = 5-
CC         methylsulfanyl-2,3-dioxopentyl phosphate + H2O;
CC         Xref=Rhea:RHEA:15549, ChEBI:CHEBI:15377, ChEBI:CHEBI:58548,
CC         ChEBI:CHEBI:58828; EC=4.2.1.109; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01677, ECO:0000256|SAAS:SAAS01115952};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01677};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01677};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via
CC       salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose
CC       1-phosphate: step 2/6. {ECO:0000256|HAMAP-Rule:MF_01677,
CC       ECO:0000256|SAAS:SAAS00548694}.
CC   -!- SIMILARITY: Belongs to the aldolase class II family. MtnB
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01677}.
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DR   EMBL; CT978603; CAK27352.1; -; Genomic_DNA.
DR   STRING; 316278.SynRCC307_0449; -.
DR   EnsemblBacteria; CAK27352; CAK27352; SynRCC307_0449.
DR   KEGG; syr:SynRCC307_0449; -.
DR   eggNOG; ENOG4107QY0; Bacteria.
DR   eggNOG; COG0235; LUCA.
DR   HOGENOM; HOG000086153; -.
DR   KO; K08964; -.
DR   OMA; GHGLYTW; -.
DR   BioCyc; SSP316278:G1GJL-447-MONOMER; -.
DR   UniPathway; UPA00904; UER00875.
DR   Proteomes; UP000001115; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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   Gene3D; 3.40.225.10; -; 1.
DR   HAMAP; MF_01677; Salvage_MtnB; 1.
DR   InterPro; IPR001303; Aldolase_II/adducin_N.
DR   InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR   InterPro; IPR017714; MethylthioRu-1-P_deHdtase_MtnB.
DR   PANTHER; PTHR10640; PTHR10640; 1.
DR   Pfam; PF00596; Aldolase_II; 1.
DR   SMART; SM01007; Aldolase_II; 1.
DR   SUPFAM; SSF53639; SSF53639; 1.
DR   TIGRFAMs; TIGR03328; salvage_mtnB; 1.
PE   3: Inferred from homology;
DR   PRODOM; A5GR43.
DR   SWISS-2DPAGE; A5GR43.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01677,
KW   ECO:0000256|SAAS:SAAS00548699};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001115};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01677,
KW   ECO:0000256|SAAS:SAAS00548696};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01677,
KW   ECO:0000256|SAAS:SAAS00548706};
KW   Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01677,
KW   ECO:0000256|SAAS:SAAS00548698};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001115};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01677, ECO:0000256|SAAS:SAAS00548703}.
FT   DOMAIN       26    214       Aldolase_II. {ECO:0000259|SMART:SM01007}.
FT   METAL       113    113       Zinc. {ECO:0000256|HAMAP-Rule:MF_01677}.
FT   METAL       115    115       Zinc. {ECO:0000256|HAMAP-Rule:MF_01677}.
SQ   SEQUENCE   226 AA;  24250 MW;  078D42AFC690A5C1 CRC64;
     MRHDPAARHT GGTKQSLVSK LSALRQELVD VMADVHRRGW CDGTGGNFSC LMSREPLQLV
     MAPSGVHKGN VSADELIVVD GNAAVIEGTG KASAETLLHL TIVRSCAAGA VLHSHSQAGT
     LLSQWALPRG HLKLQDLEML KGLAEVSTHQ SSVSVPVLAN DQDLQRLSEA AQPHLAGAPH
     GLLIAGHGLY AWGEDLFSAT RHLEILEFLL EQRWRQLLLQ GLGVQP
//

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