ID A0A0N1NUB1_9ACTN Unreviewed; 389 AA.
AC A0A0N1NUB1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Hydroxymethylglutaryl-CoA synthase {ECO:0000313|EMBL:KPI32436.1};
DE EC=2.3.3.10 {ECO:0000313|EMBL:KPI32436.1};
GN ORFNames=OV320_2119 {ECO:0000313|EMBL:KPI32436.1};
OS Actinobacteria bacterium OV320.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592329 {ECO:0000313|EMBL:KPI32436.1, ECO:0000313|Proteomes:UP000037870};
RN [1] {ECO:0000313|EMBL:KPI32436.1, ECO:0000313|Proteomes:UP000037870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV320 {ECO:0000313|EMBL:KPI32436.1,
RC ECO:0000313|Proteomes:UP000037870};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. HMG-CoA synthase
CC family. {ECO:0000256|ARBA:ARBA00007061}.
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:KPI32436.1}.
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DR EMBL; LJCX01000003; KPI32436.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1NUB1; -.
DR PATRIC; fig|1592329.3.peg.690; -.
DR Proteomes; UP000037870; Unassembled WGS sequence.
DR GO; GO:0004421; F:hydroxymethylglutaryl-CoA synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:InterPro.
DR GO; GO:0010142; P:farnesyl diphosphate biosynthetic process, mevalonate pathway; IEA:InterPro.
DR CDD; cd00827; init_cond_enzymes; 1.
DR Gene3D; 3.40.47.10; -; 2.
DR InterPro; IPR013746; HMG_CoA_synt_C_dom.
DR InterPro; IPR013528; HMG_CoA_synth_N.
DR InterPro; IPR011554; HMG_CoA_synthase_prok.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; TIGR01835; HMG-CoA-S_prok; 1.
DR PANTHER; PTHR43323; 3-HYDROXY-3-METHYLGLUTARYL COENZYME A SYNTHASE; 1.
DR PANTHER; PTHR43323:SF2; HYDROXYMETHYLGLUTARYL-COA SYNTHASE; 1.
DR Pfam; PF08540; HMG_CoA_synt_C; 2.
DR Pfam; PF01154; HMG_CoA_synt_N; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:KPI32436.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037870};
KW Transferase {ECO:0000313|EMBL:KPI32436.1}.
FT DOMAIN 5..167
FT /note="Hydroxymethylglutaryl-coenzyme A synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01154"
FT DOMAIN 177..250
FT /note="Hydroxymethylglutaryl-coenzyme A synthase C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08540"
FT DOMAIN 266..325
FT /note="Hydroxymethylglutaryl-coenzyme A synthase C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08540"
FT REGION 353..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 81
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR611554-1"
FT ACT_SITE 113
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR611554-1"
FT ACT_SITE 235
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR611554-1"
FT BINDING 145
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR611554-2"
FT BINDING 244
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR611554-2"
FT BINDING 278
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR611554-2"
SQ SEQUENCE 389 AA; 41705 MW; 58D7C0455AE03EC6 CRC64;
MSLSIGIHDL SFATAEFVLP HTELAAHNGT EIGKYHIGIG QESMSIPGAD EDIVTMAAAA
AAPVIARHGS DRIRTVVFAT ESSIDQAKAA GIYVHSLLGL PSATRIVELK QACYGATAAL
QFAIGLVRRD PAQQVLVIAS DVSKYELDSP GEATQGAAAV AMLVGADPAL VRIEDPSGLF
TADVMDFWRP NYRNEALVDG HESINAYLQA VEGTWKDYTE QGGRALEEFA AFCYHQPFTK
MAYKAHRHLL NYCGQDTDND AVSAAIGRTT AYNTVIGNSY TASVYLALAA LLDQGDDLTG
KAIGFLSYGS GSVAEFFAGT VTAGYRDNLR TDANREAIAR RTPVDLAGYR DLHERSFPTD
GGDHATERHT SGPFRLAGIS GHKRLYQAR
//