ID A0A1K1MQW5_9BACL Unreviewed; 426 AA.
AC A0A1K1MQW5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=2,3-diketo-5-methylthiopentyl-1-phosphate enolase {ECO:0000313|EMBL:SFW25465.1};
GN ORFNames=SAMN02799630_01398 {ECO:0000313|EMBL:SFW25465.1};
OS Paenibacillus sp. UNCCL117.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1502764 {ECO:0000313|EMBL:SFW25465.1, ECO:0000313|Proteomes:UP000182480};
RN [1] {ECO:0000313|EMBL:SFW25465.1, ECO:0000313|Proteomes:UP000182480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UNCCL117 {ECO:0000313|EMBL:SFW25465.1,
RC ECO:0000313|Proteomes:UP000182480};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FPIU01000004; SFW25465.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1K1MQW5; -.
DR STRING; 1502764.SAMN02799630_01398; -.
DR Proteomes; UP000182480; Unassembled WGS sequence.
DR GO; GO:0043715; F:2,3-diketo-5-methylthiopentyl-1-phosphate enolase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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:InterPro.
DR CDD; cd08209; RLP_DK-MTP-1-P-enolase; 1.
DR Gene3D; 3.20.20.110; Ribulose bisphosphate carboxylase, large subunit, C-terminal domain; 1.
DR Gene3D; 3.30.70.150; RuBisCO large subunit, N-terminal domain; 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; IPR036422; RuBisCO_lsu_N_sf.
DR NCBIfam; TIGR03332; salvage_mtnW; 1.
DR PANTHER; PTHR42704; RIBULOSE BISPHOSPHATE CARBOXYLASE; 1.
DR PANTHER; PTHR42704:SF9; RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN; 1.
DR Pfam; PF00016; RuBisCO_large; 1.
DR SFLD; SFLDF00157; 2_3-diketo-5-methylthiopentyl; 1.
DR SFLD; SFLDG00301; RuBisCO-like_proteins; 1.
DR SUPFAM; SSF51649; RuBisCo, C-terminal domain; 1.
DR SUPFAM; SSF54966; RuBisCO, large subunit, small (N-terminal) domain; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW Reference proteome {ECO:0000313|Proteomes:UP000182480}.
FT DOMAIN 131..422
FT /note="Ribulose bisphosphate carboxylase large subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF00016"
SQ SEQUENCE 426 AA; 45869 MW; 289B75BF37EFBE46 CRC64;
MNLQAYQTYC VATYRAYDDK ADFQKKALGI AVGLTVGSWT DLPEARKAEM EKHLGQVVDV
TVHEPDSRQP GERYADIQIA YPDVNFSRDI PALLVTVFGK LSMDGRIKLI DLSFSDGFLS
AFPGPRFGLP GVRQLLGVQD RPLLMSIFKS VIGHDLPALR EQFYQQALGG VDLIKDDEIL
FENPLTPIER RVEVCMEAAA QAQRETGQKL LYAANLTGPT FDLVEQAKRA IGAGANALLF
NVLAYGFDAL SELSRHPDVN VPIMAHPALA GAFYPSTYHG ISANVLLGKL MRLAGADLVL
FPSPYGSVVM PLEENMAIKD ALLTTQASDY ALGASADRTL ALARSFPVPS AGIHPGLVPW
ILRDFGHDVV VNAGGGVHGH PQGAAAGGRA FRQAIEACLS GIPLRAFAAD GHPELQAAIE
AWGIKE
//