ID   HBOH_ALBFT              Reviewed;         704 AA.
AC   Q21U20;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=Rfer_3022;
OS   Albidiferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118)
OS   (Rhodoferax ferrireducens).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Rhodoferax.
OX   NCBI_TaxID=338969;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-621 / DSM 15236 / T118;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of chromosome of Rhodoferax ferrireducens DSM 15236.";
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000267; ABD70733.1; -; Genomic_DNA.
DR   RefSeq; WP_011465299.1; NC_007908.1.
DR   AlphaFoldDB; Q21U20; -.
DR   STRING; 338969.Rfer_3022; -.
DR   ESTHER; rhoft-hboh; OHBut_olig_hydro_put.
DR   EnsemblBacteria; ABD70733; ABD70733; Rfer_3022.
DR   KEGG; rfr:Rfer_3022; -.
DR   eggNOG; ENOG502Z8QU; Bacteria.
DR   HOGENOM; CLU_420258_0_0_4; -.
DR   OMA; NPEKDWG; -.
DR   OrthoDB; 865015at2; -.
DR   UniPathway; UPA00863; -.
DR   Proteomes; UP000008332; Chromosome.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0047989; F:hydroxybutyrate-dimer hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019605; P:butyrate metabolic process; IEA:UniProtKB-UniRule.
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; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01906"
FT   CHAIN           32..704
FT                   /note="D-(-)-3-hydroxybutyrate oligomer hydrolase"
FT                   /id="PRO_5000110604"
FT   ACT_SITE        309
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01906"
SQ   SEQUENCE   704 AA;  71951 MW;  3C7477A6937EC189 CRC64;
     MTTTNRNNLK LTALTAAVLT LSACGGSDAV AENKNVKPAY LGEVASASYD GISDDLLTAG
     LGKTGLGGAA PAVVDPLSPT SAELRKLAIF NNYRAILDIT AGGGYGTLYG PNVDAKGVVG
     ASEGMIAGTE YIAYSDDGTG RQNITMMVQV PATFNPASPC IVTATSSGSR GVYGAIGSSG
     EWGLKNGCAV AYTDKGTGTG IHDLQNDTVN VQNGGRASAT AAGKASIFTA LLTSIERAAF
     NLATPNRFAI KHAHSQQNPE KDWGKWTLQS VEFAYFVLNQ KYGDLASDGV AHLKKLTPAN
     TIVIASSVSN GAGAALAAAE QDTQGLISGV AVAEPEVQLA PDARLSIVRG TTTLVGTGKQ
     LLDYFTLANL LQPCAALVSP STNVFNTVNA AIAGNRCSAL KANGLITGTT TAEQAASAMA
     ALVAAGWQPE SSDLQASHYS FATLPVALTY ANTYGRFGVA DNLCGFSYAA TGAATSATPL
     APVPASAAVL ATSFGTSNGV PPTAGINIVN NNSVGGPLLD AASLSVGGVQ DYNIAGALCL
     RGLVTGTSAN AVRVQQGMSE VLRSANLHGK PALIVQGRSD TLLPVAFTGR PYFGMNKIVE
     GANSRLSYIE VTNAQHFDAF LGFPGYANRL VPLHRYFIQA MDMMYANLKT GAALPTSQVV
     RTVPRGLAGT AANPITAANV PPIKAVADVA DQITFANNVV TVAD