ID E1QE21_DESB2 Unreviewed; 292 AA.
AC E1QE21;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Pyruvate carboxyltransferase {ECO:0000313|EMBL:ADK83807.1};
GN OrderedLocusNames=Deba_0433 {ECO:0000313|EMBL:ADK83807.1};
OS Desulfarculus baarsii (strain ATCC 33931 / DSM 2075 / LMG 7858 / VKM B-1802
OS / 2st14).
OC Bacteria; Thermodesulfobacteriota; Desulfarculia; Desulfarculales;
OC Desulfarculaceae; Desulfarculus.
OX NCBI_TaxID=644282 {ECO:0000313|EMBL:ADK83807.1, ECO:0000313|Proteomes:UP000009047};
RN [1] {ECO:0000313|EMBL:ADK83807.1, ECO:0000313|Proteomes:UP000009047}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33931 / DSM 2075 / LMG 7858 / VKM B-1802 / 2st14
RC {ECO:0000313|Proteomes:UP000009047};
RX PubMed=21304732; DOI=10.4056/sigs.1243258;
RA Sun H., Spring S., Lapidus A., Davenport K., Del Rio T.G., Tice H.,
RA Nolan M., Copeland A., Cheng J.F., Lucas S., Tapia R., Goodwin L.,
RA Pitluck S., Ivanova N., Pagani I., Mavromatis K., Ovchinnikova G., Pati A.,
RA Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA Han C., Rohde M., Brambilla E., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Land M.;
RT "Complete genome sequence of Desulfarculus baarsii type strain (2st14).";
RL Stand. Genomic Sci. 3:276-284(2010).
CC -!- SIMILARITY: Belongs to the HMG-CoA lyase family.
CC {ECO:0000256|ARBA:ARBA00009405}.
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; CP002085; ADK83807.1; -; Genomic_DNA.
DR RefSeq; WP_013257263.1; NC_014365.1.
DR AlphaFoldDB; E1QE21; -.
DR STRING; 644282.Deba_0433; -.
DR KEGG; dbr:Deba_0433; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_022138_3_2_7; -.
DR Proteomes; UP000009047; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016833; F:oxo-acid-lyase activity; IEA:InterPro.
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:ADK83807.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009047}.
FT DOMAIN 1..269
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 292 AA; 30596 MW; CDCEDE374A88F2B8 CRC64;
MLEDQTLRDG LQILPRALPL ARRLELLRGL ADAGFQSVQI GSMARPDKMP QMIGAERLAR
LAAGARPGLT LSALVFNRQG LERALACGLG KVALSASLSE PHSRANLGLD VAGGLARLGE
LTALARQAGL RARVGLQCAF GGPGLAAPPR ELIARTFAWL ADLGAQEFFL ADTAGLARPN
QLRRMIAELG RNLPLEALGL HLHGRPEALR ANLLAGWRAG VGRFDVTLGG LGGCPFLPGR
APGNLPAELA IAALQAAGAP PAIDPRAVEN LGRRLRAMLD ENIPPVYSAM AS
//
