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Database: UniProt
Entry: I9LGR6_9FIRM
LinkDB: I9LGR6_9FIRM
Original site: I9LGR6_9FIRM 
ID   I9LGR6_9FIRM            Unreviewed;       302 AA.
AC   I9LGR6;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Pyruvate carboxyltransferase {ECO:0000313|EMBL:EIW19694.1};
GN   ORFNames=FB4_2613 {ECO:0000313|EMBL:EIW19694.1};
OS   Pelosinus fermentans B4.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Pelosinus.
OX   NCBI_TaxID=1149862 {ECO:0000313|EMBL:EIW19694.1, ECO:0000313|Proteomes:UP000004324};
RN   [1] {ECO:0000313|EMBL:EIW19694.1, ECO:0000313|Proteomes:UP000004324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:EIW19694.1,
RC   ECO:0000313|Proteomes:UP000004324};
RX   PubMed=22933770; DOI=10.1128/JB.01174-12;
RA   Brown S.D., Podar M., Klingeman D.M., Johnson C.M., Yang Z.K.,
RA   Utturkar S.M., Land M.L., Mosher J.J., Hurt R.A.Jr., Phelps T.J.,
RA   Palumbo A.V., Arkin A.P., Hazen T.C., Elias D.A.;
RT   "Draft Genome Sequences for Two Metal-Reducing Pelosinus fermentans Strains
RT   Isolated from a Cr(VI)-Contaminated Site and for Type Strain R7.";
RL   J. Bacteriol. 194:5147-5148(2012).
CC   -!- SIMILARITY: Belongs to the HMG-CoA lyase family.
CC       {ECO:0000256|ARBA:ARBA00009405}.
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:EIW19694.1}.
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DR   EMBL; AKVJ01000013; EIW19694.1; -; Genomic_DNA.
DR   RefSeq; WP_007932200.1; NZ_AKVJ01000013.1.
DR   AlphaFoldDB; I9LGR6; -.
DR   PATRIC; fig|1149862.3.peg.1162; -.
DR   OrthoDB; 9784013at2; -.
DR   Proteomes; UP000004324; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016833; F:oxo-acid-lyase activity; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   CDD; cd07938; DRE_TIM_HMGL; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR043594; HMGL.
DR   InterPro; IPR000891; PYR_CT.
DR   PANTHER; PTHR42738; HYDROXYMETHYLGLUTARYL-COA LYASE; 1.
DR   PANTHER; PTHR42738:SF7; HYDROXYMETHYLGLUTARYL-COA LYASE; 1.
DR   Pfam; PF00682; HMGL-like; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Pyruvate {ECO:0000313|EMBL:EIW19694.1};
KW   Transferase {ECO:0000313|EMBL:EIW19694.1}.
FT   DOMAIN          8..275
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   302 AA;  32379 MW;  8965AF398A3DC0E9 CRC64;
     MLAFPKQVQI VEVGPRDGFQ NIKTFIETKV KQQVIDGIIA AGVQAMEVTS FVHPKAIPQM
     VDAAQIAKAA AQAAGDTFRG LALIPNLTGA KKAYECGIRE VTYVISASEQ HNLANINRTR
     EQSLEDLQKI VTQVPELAVR LDVATAFGCP LGGKVDDEMV VSLIESALQI GVQSVVLCDT
     IGVAHPKQVY ERARTVKNRF SDVSFGLHLH DTRGMGLANT LAGLDAGITI FESSIGGLGG
     CPFAPGAAGN TATEDLVNMF HGMGISTGID LERYLAVVQM VREKIQDVLT GHMAYARQYD
     DI
//
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