ID A0A1H4KY74_9BACL Unreviewed; 421 AA.
AC A0A1H4KY74;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=2,3-diketo-5-methylthiopentyl-1-phosphate enolase {ECO:0000313|EMBL:SEB63045.1};
GN ORFNames=SAMN05443246_1370 {ECO:0000313|EMBL:SEB63045.1};
OS Paenibacillus sp. GP183.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1882751 {ECO:0000313|EMBL:SEB63045.1, ECO:0000313|Proteomes:UP000199177};
RN [1] {ECO:0000313|EMBL:SEB63045.1, ECO:0000313|Proteomes:UP000199177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GP183 {ECO:0000313|EMBL:SEB63045.1,
RC ECO:0000313|Proteomes:UP000199177};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FNSW01000001; SEB63045.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H4KY74; -.
DR STRING; 1882751.SAMN05443246_1370; -.
DR OrthoDB; 9770811at2; -.
DR Proteomes; UP000199177; 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:UP000199177}.
FT DOMAIN 125..417
FT /note="Ribulose bisphosphate carboxylase large subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF00016"
SQ SEQUENCE 421 AA; 45463 MW; 43E893E9D3E4296F CRC64;
MSAYCLATYR CFDEKADFAK KAAGIAVGLT VGSWTELPEA QKAQMEKHLG KVISVAVHEP
ENGQPTSERY ADIQIAYPDV NFSRDIPALL VTVFGKLSMD GKIKLTDLSF SSEFLSVFPG
PKFGLQGVRN LLGVHDRPLL MSIFKSVIGY EMAALREQFY LQAAGGVDLI KDDEILFENP
LTPLEKRVET CMEAAAQASR ETGQKLLYAA NITGPTSMLA DQAKKAIRAG ANAILFNVLA
YGFDALHELS SDPEIQVPIM AHPAMAGAFY PSPHYGISAS VLLGKLMRMA GADLVLFPSP
YGSVVMPREE NLAIKHALLT SDLARDYLYD STGSEVSLPS SFPVPSAGIH PGLVPLILRD
FGSEVIVNAG GGIHGHPQGT IAGGKAFRQA IEASLKRIPL REHAKSHQEL QIAIDTWGIK
E
//
