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Database: UniProt
Entry: I3UD02_ADVKW
LinkDB: I3UD02_ADVKW
Original site: I3UD02_ADVKW 
ID   I3UD02_ADVKW            Unreviewed;       312 AA.
AC   I3UD02;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=HMGL-like family protein {ECO:0000313|EMBL:AFK62890.1};
GN   OrderedLocusNames=TKWG_14050 {ECO:0000313|EMBL:AFK62890.1};
OS   Advenella kashmirensis (strain DSM 17095 / LMG 22695 / WT001)
OS   (Tetrathiobacter kashmirensis).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae.
OX   NCBI_TaxID=1036672 {ECO:0000313|EMBL:AFK62890.1, ECO:0000313|Proteomes:UP000005267};
RN   [1] {ECO:0000313|EMBL:AFK62890.1, ECO:0000313|Proteomes:UP000005267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17095 / LMG 22695 / WT001
RC   {ECO:0000313|Proteomes:UP000005267};
RX   PubMed=21914874; DOI=10.1128/JB.05781-11;
RA   Ghosh W., George A., Agarwal A., Raj P., Alam M., Pyne P., Das Gupta S.K.;
RT   "Whole-genome shotgun sequencing of the sulfur-oxidizing chemoautotroph
RT   Tetrathiobacter kashmirensis.";
RL   J. Bacteriol. 193:5553-5554(2011).
CC   -!- SIMILARITY: Belongs to the HMG-CoA lyase family.
CC       {ECO:0000256|ARBA:ARBA00009405}.
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DR   EMBL; CP003555; AFK62890.1; -; Genomic_DNA.
DR   RefSeq; WP_014750981.1; NC_017964.1.
DR   AlphaFoldDB; I3UD02; -.
DR   STRING; 1036672.TKWG_14050; -.
DR   KEGG; aka:TKWG_14050; -.
DR   HOGENOM; CLU_022138_3_2_4; -.
DR   OrthoDB; 9784013at2; -.
DR   Proteomes; UP000005267; Chromosome.
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   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          4..271
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   312 AA;  33670 MW;  7AE7202A3152C2D4 CRC64;
     MKKLFIQEVA PRDGFQNEAR FIETDDKIAF IDQLSQCGYA KIEVTSFTSP KAIPALKDAE
     AVMHRIRRNP DVVYTVLVPN LRGAERAMSC GVDEVNLVMS VSETHNLSNL RMSRERSFEQ
     LAAVIGEVRP TSTAINVSLS TVFGCPMQGD VALDEVVAWV DRFAQLGVDG VTLCDTTGMA
     YPTQVGSLFG AVLARFPNLQ VTAHFHNTRG MALANTVTAL QAGVVRFDSS LGGLGGCPYA
     PGASGNVTTE DMVHMLELMG YDTGINLEGI LAISRSLVPL IGHDVNSQTL AAGTRMALHP
     VPDYVRQLQQ AQ
//
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