HBOH_MARN8
ID HBOH_MARN8 Reviewed; 700 AA.
AC A1TWS1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=D-(-)-3-hydroxybutyrate oligomer hydrolase {ECO:0000255|HAMAP-Rule:MF_01906};
DE Short=3HB-oligomer hydrolase {ECO:0000255|HAMAP-Rule:MF_01906};
DE Short=3HBOH {ECO:0000255|HAMAP-Rule:MF_01906};
DE EC=3.1.1.22 {ECO:0000255|HAMAP-Rule:MF_01906};
DE Flags: Precursor;
GN OrderedLocusNames=Maqu_0083;
OS Marinobacter nauticus (strain ATCC 700491 / DSM 11845 / VT8) (Marinobacter
OS aquaeolei).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Marinobacteraceae; Marinobacter.
OX NCBI_TaxID=351348;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700491 / DSM 11845 / VT8;
RX PubMed=21335390; DOI=10.1128/aem.01866-10;
RA Singer E., Webb E.A., Nelson W.C., Heidelberg J.F., Ivanova N., Pati A.,
RA Edwards K.J.;
RT "Genomic potential of Marinobacter aquaeolei, a biogeochemical
RT 'opportunitroph'.";
RL Appl. Environ. Microbiol. 77:2763-2771(2011).
CC -!- FUNCTION: Participates in the degradation of poly-3-hydroxybutyrate
CC (PHB). It works downstream of poly(3-hydroxybutyrate) depolymerase,
CC hydrolyzing D(-)-3-hydroxybutyrate oligomers of various length (3HB-
CC oligomers) into 3HB-monomers. {ECO:0000255|HAMAP-Rule:MF_01906}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxybutanoate dimer + H2O = 2 (R)-3-hydroxybutanoate +
CC H(+); Xref=Rhea:RHEA:10172, ChEBI:CHEBI:10979, ChEBI:CHEBI:10983,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378; EC=3.1.1.22;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01906};
CC -!- PATHWAY: Lipid metabolism; butanoate metabolism. {ECO:0000255|HAMAP-
CC Rule:MF_01906}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255|HAMAP-Rule:MF_01906}.
CC -!- SIMILARITY: Belongs to the D-(-)-3-hydroxybutyrate oligomer hydrolase
CC family. {ECO:0000255|HAMAP-Rule:MF_01906}.
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DR EMBL; CP000514; ABM17190.1; -; Genomic_DNA.
DR RefSeq; WP_011783663.1; NC_008740.1.
DR AlphaFoldDB; A1TWS1; -.
DR STRING; 351348.Maqu_0083; -.
DR ESTHER; marhv-hboh; OHBut_olig_hydro_put.
DR EnsemblBacteria; ABM17190; ABM17190; Maqu_0083.
DR KEGG; maq:Maqu_0083; -.
DR eggNOG; ENOG502Z8QU; Bacteria.
DR HOGENOM; CLU_420258_0_0_6; -.
DR OMA; NPEKDWG; -.
DR OrthoDB; 865015at2; -.
DR UniPathway; UPA00863; -.
DR Proteomes; UP000000998; Chromosome.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0047989; F:hydroxybutyrate-dimer hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0019605; P:butyrate metabolic process; IEA:UniProtKB-UniPathway.
DR HAMAP; MF_01906; 3HBOH; 1.
DR InterPro; IPR016582; OHBut_olig_hydro_put.
DR Pfam; PF10605; 3HBOH; 1.
DR PIRSF; PIRSF011409; HObutyrate_olig_hydrol; 1.
PE 3: Inferred from homology;
KW Hydrolase; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01906"
FT CHAIN 22..700
FT /note="D-(-)-3-hydroxybutyrate oligomer hydrolase"
FT /id="PRO_5000208712"
FT ACT_SITE 293
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01906"
SQ SEQUENCE 700 AA; 74222 MW; FF517F646F96C11A CRC64;
MKRMMLCTLI GAATVTLTAC KKDEVFNSLP DFLVSDVRQF DYDGNTDDLL TAGLGPEGLA
SATPPAFVDA LNPTPAELRR LAIYNNYRAL VDTAPGGGYG SLFGPAVGNA SGRIPGQEFI
AMMQVPGATV PVTVMAQVPD SFDPDFPCMV TAPSSGSRGI YGAIGTAGEW GLKKGCAVVY
TDKGTGTGAH NLATNTAQSV NGTLTMEPEE ALFRADLDAQ SRDDFNSQWP DRFAWKHAHS
KQNPEADWGR HVLQSIEFGF YMLNTLHGRE LGNGETLRTI NPRNTLVIAS SVSNGGGASV
RAAEQDEKGL IDGVAVSEPN VNPAVDRSFS IRQGNGPALT EHSRSLLDYT TALAVYQGCA
NQAPGIRDLA PLNGMFNPPA TGQNICHSLF NKGLVSGATK DDWALDAQRI LNEDFGVQPE
QNLLAPVHFG LAVAQSIAMT YANAYGRAGV EDRVCGLSLA ATGSAGAVVP LAPAAEASLF
AASNGIPPSA GVNLVYDNAE GQPTSLAVSA SPSSSQVDYG LDALLCLRSL AEGRDVVTGE
PLEGAQAELH EAISRGISAV RASGDLQRKP TVFVTGRADA ILPINHTSRP YVGLNQAVEG
RHSNLRYYEI LNAHHLDVLN GFPGIGDRYV PLHHYYFQAL DLMWARLTDK QPLPPSQVVR
TVPRGSLTTP LTLANLPPIQ SEPAEADRIV FTGNQLQIPD