ID A0A0R2LBE7_9LACO Unreviewed; 420 AA.
AC A0A0R2LBE7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=3-hydroxy-3-methylglutaryl coenzyme A reductase {ECO:0000313|EMBL:GEK28852.1};
DE SubName: Full=Hydroxymethylglutaryl-CoA reductase {ECO:0000313|EMBL:KRN95997.1};
GN Name=mvaA {ECO:0000313|EMBL:GEK28852.1};
GN ORFNames=IV55_GL001670 {ECO:0000313|EMBL:KRN95997.1}, LSI01_11630
GN {ECO:0000313|EMBL:GEK28852.1};
OS Furfurilactobacillus siliginis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Furfurilactobacillus.
OX NCBI_TaxID=348151 {ECO:0000313|EMBL:KRN95997.1, ECO:0000313|Proteomes:UP000051139};
RN [1] {ECO:0000313|EMBL:KRN95997.1, ECO:0000313|Proteomes:UP000051139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22696 {ECO:0000313|EMBL:KRN95997.1,
RC ECO:0000313|Proteomes:UP000051139};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
RN [2] {ECO:0000313|EMBL:GEK28852.1, ECO:0000313|Proteomes:UP000321429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101315 {ECO:0000313|EMBL:GEK28852.1,
RC ECO:0000313|Proteomes:UP000321429};
RA Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT "Whole genome shotgun sequence of Lactobacillus siliginis NBRC 101315.";
RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the HMG-CoA reductase family.
CC {ECO:0000256|ARBA:ARBA00007661}.
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:KRN95997.1}.
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DR EMBL; BJUD01000021; GEK28852.1; -; Genomic_DNA.
DR EMBL; JQCB01000006; KRN95997.1; -; Genomic_DNA.
DR RefSeq; WP_057810181.1; NZ_JQCB01000006.1.
DR AlphaFoldDB; A0A0R2LBE7; -.
DR STRING; 348151.IV55_GL001670; -.
DR PATRIC; fig|348151.3.peg.1722; -.
DR OrthoDB; 9764892at2; -.
DR Proteomes; UP000051139; Unassembled WGS sequence.
DR Proteomes; UP000321429; Unassembled WGS sequence.
DR GO; GO:0004420; F:hydroxymethylglutaryl-CoA reductase (NADPH) activity; IEA:InterPro.
DR GO; GO:0015936; P:coenzyme A metabolic process; IEA:InterPro.
DR Gene3D; 1.10.8.660; -; 1.
DR Gene3D; 3.30.70.420; Hydroxymethylglutaryl-CoA reductase, class I/II, NAD/NADP-binding domain; 1.
DR InterPro; IPR002202; HMG_CoA_Rdtase.
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 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; PS00318; HMG_COA_REDUCTASE_2; 1.
DR PROSITE; PS01192; HMG_COA_REDUCTASE_3; 1.
DR PROSITE; PS50065; HMG_COA_REDUCTASE_4; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000051139}.
SQ SEQUENCE 420 AA; 44211 MW; 017FD5B2EABB4817 CRC64;
MNLAASLRNF RKLDWDARVA VATELGQLDS SSQQQLLAHF DERDALLIEN YLTNYQLPTG
LAATIRMNDQ DYLVPMVTEE PSVIAAASYG GKMTSTGAGI ITSMPTNLLM GQVVFQTVTQ
AEVSRFVDPQ VDALLALANA AHPSILTHGG GAKKIRVRAL GEGFVSVDLF VDTGAAMGAN
MMNGMLEALG HHLQDVLEQH PVMSILTNDG QGSLVTATVT VAVANLAKGN VTAGLQVAKR
IVAASDIAQL DVSRATTHNK GIMNGVDAAV VASGNDWRAV EASAHAYAAH SGQYRGLSRW
SLQDERLEGV LTMPMHLGLV GGATGSLPLA KINQQISQVA SVATLNQLVV AVGLAQNLAA
LRALVSEGIQ QGHMHLQYRN LALVAGATPT QVPQVVDALG QQATADLAAA KRIVNQLNEQ
//
