ID R2XGK1_9ENTE Unreviewed; 410 AA.
AC R2XGK1;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=2,3-diketo-5-methylthiopentyl-1-phosphate enolase {ECO:0008006|Google:ProtNLM};
GN ORFNames=UKC_03912 {ECO:0000313|EMBL:EOI53959.1};
OS Enterococcus gilvus ATCC BAA-350.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1158614 {ECO:0000313|EMBL:EOI53959.1, ECO:0000313|Proteomes:UP000013750};
RN [1] {ECO:0000313|EMBL:EOI53959.1, ECO:0000313|Proteomes:UP000013750}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-350 {ECO:0000313|EMBL:EOI53959.1,
RC ECO:0000313|Proteomes:UP000013750};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A.M., Gilmore M.S., Lebreton F., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Enterococcus gilvus ATCC BAA-350.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family.
CC {ECO:0000256|RuleBase:RU003834}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EOI53959.1}.
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DR EMBL; AJDQ01000012; EOI53959.1; -; Genomic_DNA.
DR RefSeq; WP_010782240.1; NZ_KB946874.1.
DR AlphaFoldDB; R2XGK1; -.
DR PATRIC; fig|1158614.3.peg.3906; -.
DR eggNOG; COG1850; Bacteria.
DR HOGENOM; CLU_031450_3_1_9; -.
DR OrthoDB; 9770811at2; -.
DR Proteomes; UP000013750; Unassembled WGS sequence.
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:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd08205; RuBisCO_IV_RLP; 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; 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; RIBULOSE BISPHOSPHATE CARBOXYLASE; 1.
DR PANTHER; PTHR42704:SF9; RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN; 1.
DR Pfam; PF00016; RuBisCO_large; 1.
DR Pfam; PF02788; RuBisCO_large_N; 1.
DR SFLD; SFLDS00014; RuBisCO; 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 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167}.
FT DOMAIN 16..119
FT /note="Ribulose bisphosphate carboxylase large subunit
FT ferrodoxin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02788"
FT DOMAIN 130..409
FT /note="Ribulose bisphosphate carboxylase large subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF00016"
SQ SEQUENCE 410 AA; 43648 MW; A4AEC332E943BC51 CRC64;
MKFETLKMAE GLGQDFLIAT YYMHSEKEPD LYDWVKLVAG DQSAGTWTHV EGETPEVIER
YGAKVLGIYP MSDGISCVAR VAFPITNFQP YMAMVISTVA GNVLGQSGIR LVDVEFPESL
LKEFTGPLLG VSGIRKKLGV MDRPLVGAIL KPCIGVPPEA SAQGAANAAL GGADVIKDDE
LLSDPAYSPM VDRVKTVMSY LKEVGKEQST LYAVNITGRN IIERAQLAIE AGANALMVNY
NALGWGATED LVRFLKDQNV EIPIFGHCAG AGAYYKAENN GLSAALSCGK LPRLIGMDMP
LVYPDSGRFG TTTDELVETH SALSTPMQGI ESAFTTVAGG VHPGTIEYLM GLLGNETILM
AGGGIYGHPA GAVSGAKALL QAIEAVMQEV PVTEAAQTYE ELQQALAFWS
//
