ID A0A0Q4IS99_9SPHN Unreviewed; 303 AA.
AC A0A0Q4IS99;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=3-hydroxy-3-methylglutaryl-CoA lyase {ECO:0000313|EMBL:KQN00657.1};
GN ORFNames=ASE85_08370 {ECO:0000313|EMBL:KQN00657.1};
OS Sphingobium sp. Leaf26.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1735693 {ECO:0000313|EMBL:KQN00657.1, ECO:0000313|Proteomes:UP000051336};
RN [1] {ECO:0000313|Proteomes:UP000051336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf26 {ECO:0000313|Proteomes:UP000051336};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000051336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf26 {ECO:0000313|Proteomes:UP000051336};
RA Vorholt J.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQN00657.1}.
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DR EMBL; LMKV01000023; KQN00657.1; -; Genomic_DNA.
DR RefSeq; WP_056689485.1; NZ_LMKV01000023.1.
DR AlphaFoldDB; A0A0Q4IS99; -.
DR STRING; 1735693.ASE85_08370; -.
DR OrthoDB; 9784013at2; -.
DR Proteomes; UP000051336; 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:KQN00657.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 4..271
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 303 AA; 31557 MW; A2A4BB4FEC59AEB1 CRC64;
MRRIELVEVG PRDGLQNESL IVSTADKVAL VGRALAAGVR RIEVASFVNP RRVPQMADAE
TVIAALPDRD DAIYVGLVLN VRGAKRALLT KVDELGAVCV ASDSFAMRNQ GQTSAESVQS
ARDIIALAKA AGRSAQVTIG AAFGCPFEGF VSPDHVVAMA VELAKSGPRE IALADTIGVA
VPAEVTALVT RVRAAVPDMP IRCHFHDTRN TGLANVWAAV EAGATTIDAS LGGLGGCPFA
PGAAGNVSTE DVQYLLERSG IATGVDLDML IDANRWFTTV MGKPLPSMVA RAGAFPSANQ
SEQ
//
