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Database: UniProt
Entry: A0A081PDT6_9SPHI
LinkDB: A0A081PDT6_9SPHI
Original site: A0A081PDT6_9SPHI 
ID   A0A081PDT6_9SPHI        Unreviewed;       283 AA.
AC   A0A081PDT6;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Hydroxymethylglutaryl-CoA lyase {ECO:0000313|EMBL:KEQ28859.1};
GN   ORFNames=N180_20225 {ECO:0000313|EMBL:KEQ28859.1};
OS   Pedobacter antarcticus 4BY.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=1358423 {ECO:0000313|EMBL:KEQ28859.1, ECO:0000313|Proteomes:UP000028007};
RN   [1] {ECO:0000313|EMBL:KEQ28859.1, ECO:0000313|Proteomes:UP000028007}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4BY {ECO:0000313|EMBL:KEQ28859.1,
RC   ECO:0000313|Proteomes:UP000028007};
RA   Shivaji S., Ray M.K., Rao N.S., Saiserr L., Jagannadham M.V., Kumar G.S.,
RA   Reddy G., Bhargava P.M.;
RT   "Sphingobacterium antarcticus sp. nov. a Psychrotrophic Bacterium from the
RT   Soils of Schirmacher Oasis, Antarctica.";
RL   Int. J. Syst. Bacteriol. 42:102-106(1992).
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:KEQ28859.1}.
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DR   EMBL; JNFF01000099; KEQ28859.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A081PDT6; -.
DR   eggNOG; COG0119; Bacteria.
DR   Proteomes; UP000028007; 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   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   Lyase {ECO:0000313|EMBL:KEQ28859.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028007}.
FT   DOMAIN          1..270
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   283 AA;  31152 MW;  1CDE16E420B07015 CRC64;
     MKLVECPRDA MQGIHEFIPT ALKAAYINLL LKAGFDTLDF GSFVSSKAIP QMQDTKDVLE
     KLDLSSTSTK LLAIAANLRG AEEAVACPEI SYVGFPFSIS ETFQHRNTNS SMLASLNTVD
     QILELCDRHQ KTAVIYLSMG FGNPYGDPYS FDIVGEWASS LAGLGTKILS LADTTGVSTA
     EQIRILMPML QKQFPDIECG LHLHSTPEKR IEKITAAYES GCRRFDSALR GFGGCPMAKD
     DLTGNIATEE LLAFLESRKE STGINDYYWN EALQLSTEVF SYN
//
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