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Database: UniProt
Entry: J1Q386_9ALTE
LinkDB: J1Q386_9ALTE
Original site: J1Q386_9ALTE 
ID   J1Q386_9ALTE            Unreviewed;       304 AA.
AC   J1Q386;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Hydroxymethylglutaryl-CoA lyase {ECO:0000313|EMBL:EJI85563.1};
GN   ORFNames=AEST_14840 {ECO:0000313|EMBL:EJI85563.1};
OS   Alishewanella aestuarii B11.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alishewanella.
OX   NCBI_TaxID=1197174 {ECO:0000313|EMBL:EJI85563.1, ECO:0000313|Proteomes:UP000012043};
RN   [1] {ECO:0000313|EMBL:EJI85563.1, ECO:0000313|Proteomes:UP000012043}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B11 {ECO:0000313|EMBL:EJI85563.1,
RC   ECO:0000313|Proteomes:UP000012043};
RX   PubMed=22965096; DOI=10.1128/JB.01255-12;
RA   Jung J., Choi S., Chun J., Park W.;
RT   "Genome Sequence of Pectin-Degrading Alishewanella aestuarii Strain B11T,
RT   Isolated from Tidal Flat Sediment.";
RL   J. Bacteriol. 194:5476-5476(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:EJI85563.1}.
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DR   EMBL; ALAB01000021; EJI85563.1; -; Genomic_DNA.
DR   RefSeq; WP_008608119.1; NZ_ALAB01000021.1.
DR   AlphaFoldDB; J1Q386; -.
DR   PATRIC; fig|1197174.4.peg.1452; -.
DR   Proteomes; UP000012043; 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:EJI85563.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          7..273
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   304 AA;  31435 MW;  7149456EFFEEC56C CRC64;
     MSFPKQVRLV EVGPRDGLQN ESSVSSGAKI QLINLLSAAG HQYIEAGAFV SPKWVPQMAD
     SAQVFAGIKR HHGVTYAALT PNLQGYAAAK AAGATEVAIF GAASEAFSQK NINCSVAESL
     QRFAPVLEAA KTDGIKVRGY VSCVVGCPYQ GEVAPADVAF VAKALLDMGC YEISLGDTIG
     VGTPAKVNAM LDAVLAVVPK EQLAVHFHDT YGQALTNIYV ALSRGIAVID SAVAGLGGCP
     YADGASGNVA TEDVVYLLNG LGIAHGVDLT LLAQAGWFIT RELGKQPSSK VGLALQAKCS
     QTGQ
//
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