ID A0A101E8W3_9FIRM Unreviewed; 286 AA.
AC A0A101E8W3;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=2,3-diketo-5-methylthiopentyl-1-phosphate enolase {ECO:0000313|EMBL:KUK10964.1};
GN ORFNames=XD50_0790 {ECO:0000313|EMBL:KUK10964.1};
OS Clostridia bacterium 41_269.
OC Bacteria; Bacillota; Clostridia.
OX NCBI_TaxID=1635275 {ECO:0000313|EMBL:KUK10964.1, ECO:0000313|Proteomes:UP000053409};
RN [1] {ECO:0000313|Proteomes:UP000053409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
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:KUK10964.1}.
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DR EMBL; LGEZ01000007; KUK10964.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101E8W3; -.
DR STRING; 1635275.XD50_0790; -.
DR Proteomes; UP000053409; 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 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;
FT DOMAIN 15..131
FT /note="Ribulose bisphosphate carboxylase large subunit
FT ferrodoxin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02788"
FT DOMAIN 142..276
FT /note="Ribulose bisphosphate carboxylase large subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF00016"
SQ SEQUENCE 286 AA; 31785 MW; 601576E889122DDC CRC64;
MLDPLLYDLP DNLDKEKYII ATYYVAGKRN IDALRYSAAI AVEQSTGTWL PVPAETPELR
KKHIAKIVGI YEIPNFSWEI PEDVKERHFV VRIAFPTENF TVQFAMLLTS VIGNISSGGK
LKLLDLEMPE SWLSTFKGPK FGVEGVREIL GIPERPLVNN MIKPCAGLTP EATAQLAYEA
AVGGTDIIKD DELIADAAYS PLEVRVKKVM EALKRADDEK SEKTLYAVNI TDRVDKIKEN
AYRCLEAGAN CLMINYLTVG LDAVVMLAED PDINVPILGH PDFRGM
//
