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Database: UniProt
Entry: A0A011RRM2_9LACT
LinkDB: A0A011RRM2_9LACT
Original site: A0A011RRM2_9LACT 
ID   A0A011RRM2_9LACT        Unreviewed;       429 AA.
AC   A0A011RRM2;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
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=ADIAL_0159 {ECO:0000313|EMBL:EXJ24420.1};
OS   Alkalibacterium sp. AK22.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Alkalibacterium.
OX   NCBI_TaxID=1229520 {ECO:0000313|EMBL:EXJ24420.1, ECO:0000313|Proteomes:UP000020164};
RN   [1] {ECO:0000313|EMBL:EXJ24420.1, ECO:0000313|Proteomes:UP000020164}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK22 {ECO:0000313|Proteomes:UP000020164};
RA   Singh A., Pinnaka A.K.;
RL   Submitted (JAN-2014) 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:EXJ24420.1}.
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DR   EMBL; JANL01000006; EXJ24420.1; -; Genomic_DNA.
DR   RefSeq; WP_034298722.1; NZ_JANL01000006.1.
DR   AlphaFoldDB; A0A011RRM2; -.
DR   STRING; 1229520.ADIAL_0159; -.
DR   PATRIC; fig|1229520.3.peg.160; -.
DR   eggNOG; COG1257; Bacteria.
DR   OrthoDB; 9764892at2; -.
DR   UniPathway; UPA00257; UER00367.
DR   Proteomes; UP000020164; 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; IPR023076; HMG_CoA_Rdtase_CS.
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   SUPFAM; SSF55035; NAD-binding domain of HMG-CoA reductase; 1.
DR   SUPFAM; SSF56542; Substrate-binding domain of HMG-CoA reductase; 1.
DR   PROSITE; PS01192; HMG_COA_REDUCTASE_3; 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:UP000020164}.
SQ   SEQUENCE   429 AA;  45829 MW;  4F925F168471FB40 CRC64;
     MDTSKLSKFY RKTLHEKIES LYKAGVITEA EQTLLLEGRL DLPADTGDNM IENYLGNFSL
     PFGAAMNFVI NGQEKVIPMA IEEPSVVAAA SFAAKLAGSA GGFETTVTKR DMIGQVTLKG
     IIDYDGAERA IMNSKQAILD RANEAHPSIV KRGGGARDLE VRQLHDESQV NLPSFLSVHV
     HVDTQEAMGA NIINTMMEGI APYIEELTGG TALLRILSNY ATESLATARC TIPAHTLKTG
     HFSGEDVRDR IIEATQVATI DPYRAVTHNK GIMNGVDAVV TATGNDWRAV EASVHAFASR
     SGQYRSLTQW EKNDAGDLVG RLTLPLPIGT VGGAISIHPA AKLAHQMLGH PNAMELSGIL
     ATVGLAQNLA AVRALVTDGI QKGHMGLHAR SLAISAGAKG PEVQHVADQL KKAPHMNLEA
     ARTILNSLN
//
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