ID A0A1V8TNL4_9PEZI Unreviewed; 390 AA.
AC A0A1V8TNL4;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=hydroxymethylglutaryl-CoA lyase {ECO:0000256|ARBA:ARBA00012910};
DE EC=4.1.3.4 {ECO:0000256|ARBA:ARBA00012910};
GN ORFNames=B0A48_02305 {ECO:0000313|EMBL:OQO12841.1};
OS Rachicladosporium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX NCBI_TaxID=1507870 {ECO:0000313|EMBL:OQO12841.1, ECO:0000313|Proteomes:UP000192596};
RN [1] {ECO:0000313|Proteomes:UP000192596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5527 {ECO:0000313|Proteomes:UP000192596};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-hydroxy-3-methylglutaryl-CoA = acetoacetate + acetyl-CoA;
CC Xref=Rhea:RHEA:24404, ChEBI:CHEBI:13705, ChEBI:CHEBI:43074,
CC ChEBI:CHEBI:57288; EC=4.1.3.4;
CC Evidence={ECO:0000256|ARBA:ARBA00001651};
CC -!- PATHWAY: Metabolic intermediate metabolism; (S)-3-hydroxy-3-
CC methylglutaryl-CoA degradation; acetoacetate from (S)-3-hydroxy-3-
CC methylglutaryl-CoA: step 1/1. {ECO:0000256|ARBA:ARBA00005143}.
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:OQO12841.1}.
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DR EMBL; NAJO01000004; OQO12841.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V8TNL4; -.
DR STRING; 1507870.A0A1V8TNL4; -.
DR InParanoid; A0A1V8TNL4; -.
DR OrthoDB; 1210873at2759; -.
DR UniPathway; UPA00896; UER00863.
DR Proteomes; UP000192596; Unassembled WGS sequence.
DR GO; GO:0004419; F:hydroxymethylglutaryl-CoA lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044283; P:small molecule biosynthetic process; IEA:UniProt.
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:SF11; HYDROXYMETHYLGLUTARYL-COA LYASE; 1.
DR Pfam; PF00682; HMGL-like; 2.
DR SUPFAM; SSF51569; Aldolase; 2.
DR PROSITE; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000192596}.
FT DOMAIN 31..356
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT REGION 120..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 390 AA; 41564 MW; 966D83723EB2740F CRC64;
MAKSMRAVQC LLRPAGRRSF TTSPRALADH VRIIEVGPRD GLQNEKKSIS AETKIELVRR
LAGTGLETIE AGSFVHPKWV PQMAASDKVL ESILSSPPSA PHPITYQWLL PNSKGLDNYF
KVMGAAPPEQ PSGQDSGPAS NTSSMDPNAM PAARSGAEGM SQARSDSANT RNGHNHEVSI
FMAATEAFSK KNTNCSIQES LDRFAPLMTE AKKQGYPVRA YISVALGCPF EGPDVDPHKV
AEIAASLLEL GAEEISVADT TGMGTAPRTR KLLQTLKEAG IRNEDLALHF HDTFGQALVN
TIISLEHGVR TFDSAVGGLG GCPYSPGATG NVATEDLIYT LHSLGAKTGV DLDEMSRIGK
WITGEIGRDY NSSAGKATLS RLDRAAGPKL
//
