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Database: UniProt
Entry: A0A0P7AWZ3_9FLAO
LinkDB: A0A0P7AWZ3_9FLAO
Original site: A0A0P7AWZ3_9FLAO 
ID   A0A0P7AWZ3_9FLAO        Unreviewed;       438 AA.
AC   A0A0P7AWZ3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=3-hydroxy-3-methylglutaryl coenzyme A reductase {ECO:0000256|RuleBase:RU361219};
DE            Short=HMG-CoA reductase {ECO:0000256|RuleBase:RU361219};
DE            EC=1.1.1.88 {ECO:0000256|RuleBase:RU361219};
GN   ORFNames=I595_1085 {ECO:0000313|EMBL:KPM32659.1};
OS   Croceitalea dokdonensis DOKDO 023.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Croceitalea.
OX   NCBI_TaxID=1300341 {ECO:0000313|EMBL:KPM32659.1, ECO:0000313|Proteomes:UP000050280};
RN   [1] {ECO:0000313|EMBL:KPM32659.1, ECO:0000313|Proteomes:UP000050280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DOKDO 023 {ECO:0000313|EMBL:KPM32659.1,
RC   ECO:0000313|Proteomes:UP000050280};
RA   Kwon S.-K., Lee H.K., Kwak M.-J., Kim J.F.;
RT   "Genome sequence of the marine flavobacterium Croceitalea dokdonensis DOKDO
RT   023 that contains proton- and sodium-pumping rhodopsins.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-mevalonate + CoA + 2 NAD(+) = (3S)-hydroxy-3-
CC         methylglutaryl-CoA + 2 H(+) + 2 NADH; Xref=Rhea:RHEA:14833,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:36464, ChEBI:CHEBI:43074,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.88;
CC         Evidence={ECO:0000256|RuleBase:RU361219};
CC   -!- PATHWAY: Metabolic intermediate metabolism; (R)-mevalonate degradation;
CC       (S)-3-hydroxy-3-methylglutaryl-CoA from (R)-mevalonate: step 1/1.
CC       {ECO:0000256|RuleBase:RU361219}.
CC   -!- SIMILARITY: Belongs to the HMG-CoA reductase family.
CC       {ECO:0000256|ARBA:ARBA00007661, ECO:0000256|RuleBase:RU361219}.
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:KPM32659.1}.
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DR   EMBL; LDJX01000002; KPM32659.1; -; Genomic_DNA.
DR   RefSeq; WP_054558283.1; NZ_LDJX01000002.1.
DR   AlphaFoldDB; A0A0P7AWZ3; -.
DR   STRING; 1300341.I595_1085; -.
DR   PATRIC; fig|1300341.3.peg.1290; -.
DR   OrthoDB; 9764892at2; -.
DR   UniPathway; UPA00257; UER00367.
DR   Proteomes; UP000050280; Unassembled WGS sequence.
DR   GO; GO:0140643; F:hydroxymethylglutaryl-CoA reductase (NADH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0004420; F:hydroxymethylglutaryl-CoA reductase (NADPH) activity; IEA:InterPro.
DR   GO; GO:0015936; P:coenzyme A metabolic process; IEA:InterPro.
DR   CDD; cd00644; HMG-CoA_reductase_classII; 1.
DR   Gene3D; 1.10.8.660; -; 1.
DR   InterPro; IPR002202; HMG_CoA_Rdtase.
DR   InterPro; IPR004553; HMG_CoA_Rdtase_bac-typ.
DR   InterPro; IPR023074; HMG_CoA_Rdtase_cat_sf.
DR   InterPro; IPR009023; HMG_CoA_Rdtase_NAD(P)-bd_sf.
DR   InterPro; IPR009029; HMG_CoA_Rdtase_sub-bd_dom_sf.
DR   NCBIfam; TIGR00532; HMG_CoA_R_NAD; 1.
DR   PANTHER; PTHR10572; 3-HYDROXY-3-METHYLGLUTARYL-COENZYME A REDUCTASE; 1.
DR   PANTHER; PTHR10572:SF24; 3-HYDROXY-3-METHYLGLUTARYL-COENZYME A REDUCTASE; 1.
DR   Pfam; PF00368; HMG-CoA_red; 1.
DR   PRINTS; PR00071; HMGCOARDTASE.
DR   SUPFAM; SSF55035; NAD-binding domain of HMG-CoA reductase; 1.
DR   SUPFAM; SSF56542; Substrate-binding domain of HMG-CoA reductase; 1.
DR   PROSITE; PS50065; HMG_COA_REDUCTASE_4; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|RuleBase:RU361219};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU361219};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050280}.
SQ   SEQUENCE   438 AA;  48250 MW;  F9DBFE5A5CAF0C9B CRC64;
     MHTPIEGFSK LSKQEKIDWL ATAYTADPEA TKSLLTRYWN QDAGVQKIHD EFIENTLSNY
     YLPFAIAPNF LINNSLYAIP MAIEESSVVA AASKAAKFWL DKGGFQTTVL GTEKVGQVHF
     MYYGEKQKLQ SFIDLIQDNF RTDAAGITKS MEKRGGGISA IELRDLSGKL EGYYQLHCTF
     ETLDAMGANF INSCLEQFAK TLKKEALTYS EFTEKERNIE VVMSILSNYV PHCTVRAEVS
     CPIDQLQEGE IGNETFAKKM VQAVNIAKAE PHRAVTHNKG IMNGIDAVIL ATGNDFRAIE
     AGVHAYASKD GSYSSLTNAE ITNGIFHFWL EVPLALGTVG GLTSLHPMVK LSLEILKHPT
     AKELMQIVAV AGLAQNFAAL RSLVTTGIQK GHMKMHLLNL LNSLGANEAE KKALVTHFKT
     HTVSNAAARE ALENLRKS
//
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