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Database: UniProt
Entry: A0A1H1R5R6_9FLAO
LinkDB: A0A1H1R5R6_9FLAO
Original site: A0A1H1R5R6_9FLAO 
ID   A0A1H1R5R6_9FLAO        Unreviewed;       577 AA.
AC   A0A1H1R5R6;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
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=SAMN05216503_2651 {ECO:0000313|EMBL:SDS31144.1};
OS   Polaribacter sp. KT25b.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=1855336 {ECO:0000313|EMBL:SDS31144.1, ECO:0000313|Proteomes:UP000199117};
RN   [1] {ECO:0000313|Proteomes:UP000199117}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KT25b {ECO:0000313|Proteomes:UP000199117};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; LT629752; SDS31144.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1R5R6; -.
DR   STRING; 1855336.SAMN05216503_2651; -.
DR   OrthoDB; 9764892at2; -.
DR   UniPathway; UPA00257; UER00367.
DR   Proteomes; UP000199117; Chromosome i.
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   Gene3D; 1.20.120.450; dinb family like domain; 1.
DR   InterPro; IPR034660; DinB/YfiT-like.
DR   InterPro; IPR011463; DUF1569.
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; PF07606; DUF1569; 1.
DR   Pfam; PF00368; HMG-CoA_red; 1.
DR   SUPFAM; SSF109854; DinB/YfiT-like putative metalloenzymes; 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; PS00066; HMG_COA_REDUCTASE_1; 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:UP000199117}.
SQ   SEQUENCE   577 AA;  65218 MW;  F3BB95B63623E502 CRC64;
     MSKIIAGFSK FTKEEKIDWL TKNYFHNQTE TVNIIKQYWN IDTDLQELHD DFIENTISNF
     YMPYGVAPNF IINDREYVIP MVVEESSVVA AASLVAKFWS TRGGFKTKVI GTKKIGQVHF
     MFAGDKQDLE SYFNQNKTEL FAATASITKN MEKRGGGILS INLVDKTAKL ANYYQLHVTF
     ETKDSMGANF INSCLEAIAK KFENEDIEIV MSILSNYVPE CLVRAEVSCK IEELGGENPQ
     KFAEKFQQAV KIAEIEPYRA VTHNKGIMNG IDAVVLATGN DFRAIEAGAH AYASRSGQYS
     SLSHCSIDDG VFKFWIEIPL ALGTVGGLTA LHPMAKLSLE MLQKPSARTL MQIIAAAGLA
     QNFAALRALT TKGIQHGHMK MHLQNILNQF EANEEEKEII TVYFEKRTVS HSAVVEKLNS
     LRKPKINWIN FLDENSVRAH LSKLTLNSKP NFGLMNAQQM IEHLSAVTQI ANGNWVVNTF
     VSDEKTARRK PFLNTENELQ TGFKASFLAE EPNDLKFNSI AEAIDDLIKQ VAIFVKVFSD
     DKNRTVVHPF FGELDFEYWQ KFQVKHFTHH FKQFGLL
//
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