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}.
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; 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
//