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
//