ID A0A0F8WBH7_9EURO Unreviewed; 964 AA.
AC A0A0F8WBH7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, 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=ARAM_002010 {ECO:0000313|EMBL:KKK15185.1};
OS Aspergillus rambellii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK15185.1, ECO:0000313|Proteomes:UP000034291};
RN [1] {ECO:0000313|EMBL:KKK15185.1, ECO:0000313|Proteomes:UP000034291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK15185.1,
RC ECO:0000313|Proteomes:UP000034291};
RA Moore G.G., Beltz S.B., Mack B.M.;
RT "Draft Genome Sequences of Two Closely-Related Aflatoxigenic Aspergillus
RT Species Obtained from the Cote d'Ivoire.";
RL Submitted (FEB-2015) 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:KKK15185.1}.
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DR EMBL; JZBS01003356; KKK15185.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F8WBH7; -.
DR STRING; 308745.A0A0F8WBH7; -.
DR OrthoDB; 1210873at2759; -.
DR Proteomes; UP000034291; 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 GO; GO:0044283; P:small molecule biosynthetic process; IEA:UniProt.
DR CDD; cd06558; crotonase-like; 1.
DR CDD; cd07938; DRE_TIM_HMGL; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
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; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00378; ECH_1; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000034291}.
FT DOMAIN 374..647
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 964 AA; 104919 MW; EE445A4A3F424C47 CRC64;
MKLCHSNILN NARFVGDAMR LTPDDIVCCG PPLFHCFGLV LGFLASFCYG SSIVFPSDYF
RASSVVDALL NENPTVLLGV PTMLVAELEV LSKTGQKPRR LRTGLASGSA VSQVLMNEIR
ERMGVDKMLI AYGMTETSPV SFITSLDDPD QKRISTIGRV MPHTSAKVID KEGNILPRGQ
RGELCISGYA LQKGYWKNEE KTREVMRQDE NGVLWMYTGD EVMIDEAGYA HITGRIKDLI
IRGGENIFPR EIEDRLASHP NITEASVVGI RDERYGEVVG CFLKAAMCCH KIPDNEIRKW
SGVGYFGPNP RIMMRVKRDQ GKLDFGSVAT VRPRMMTVVG GSEDFIDPSK ERNTFPSCKV
GRPEEMQNPS LPSVRIVEVG PRDGLQNIRE SIDSATKVEL IRRLRGTGLQ TIELTSFVSP
RAIPQLADGR KIVQNSSIQQ LIQDPGLRLP VLVPNIKGLQ SALEIGVKEV AVFVSASEGF
SKANINCSVD EGLDRAQLVA YEAARAGVAV RGYVSCIFED PYDGPTALSS VLRCTRALLE
MGCYEVSLGD TLGIGSPADV RNLLEYLQSN GVPLEKLAGH FHDTYGGAMA NVWEAYNCGV
RVFDSSVAGL GGCPFAPGAK GNVASEDLVY MFQRSGVDTG INLSKLVSTG VWISTRLSKE
NSSRAGTALA AKQQSTFASK NPPSFSWILG RETEGVQLFR SGVNLKIILN RPRNGNALTT
AMISEVTFAV KNAADDPSIS RIILVGNGQF FCTGMDLARG RTPVGQGHSS SDAQYERLVN
LFEAIDQSPK VTIACLNGPA FGGGVGLAFA CDIRIAVTSA TVTLSEVKLG LCPATISKYV
IREWGVAFAR EAMLTARSVT PEELKARGLV AQVANSVEEL HLHLDRLLTH LKATSPAASC
LTKDLVRLAW AHAGQEEQTR GIKALFEAMM RPDTDGSHGV KEFQAKRPVD WDNYTLQQQL
KPKL
//
