ID   HBOH_ACIAC              Reviewed;         709 AA.
AC   A1TRI4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   25-MAY-2022, entry version 69.
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=Aave_3005;
OS   Acidovorax citrulli (strain AAC00-1) (Acidovorax avenae subsp. citrulli).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=397945;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAC00-1;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT   "Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1.";
RL   Submitted (DEC-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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABM33572.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000512; ABM33572.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041827498.1; NC_008752.1.
DR   AlphaFoldDB; A1TRI4; -.
DR   STRING; 397945.Aave_3005; -.
DR   ESTHER; aciac-hboh; OHBut_olig_hydro_put.
DR   EnsemblBacteria; ABM33572; ABM33572; Aave_3005.
DR   KEGG; aav:Aave_3005; -.
DR   eggNOG; ENOG502Z8QU; Bacteria.
DR   HOGENOM; CLU_420258_0_0_4; -.
DR   OrthoDB; 865015at2; -.
DR   UniPathway; UPA00863; -.
DR   Proteomes; UP000002596; 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..26
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01906"
FT   CHAIN           27..709
FT                   /note="D-(-)-3-hydroxybutyrate oligomer hydrolase"
FT                   /id="PRO_0000314412"
FT   REGION          58..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        305
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01906"
SQ   SEQUENCE   709 AA;  72873 MW;  DAC9BBC6786CFD67 CRC64;
     MTVFKTAPLL IAALAASSCG GGGSGAAVDY DFNVRPSYLN DLRQASYDGA GNDLLTGGLG
     RSGLQDDSPP GYAGSQPTAE ELRRNAIYVN YRALVDTTSE GGYGRLYGPN VDAQGRATSG
     EGMVAGTEAI AYSDDGSGRR NVTLMVQVPD AFDRTRPCII TATSSGSRGI YGGIPTGEWG
     LKRGCAVAYT DKGTGAAPHD LQADTVALID GTRTSATLAG TRAAFDAGLS AADLAAFNGA
     TPQRLAFKHA HSGQNPEKDW GLSTLQAVEF AFYVLNERFG DRSPGGQALR TFTPANTTVI
     ASSLSNGGGA AIAAAEQDTR GLIDGVAVSE PSVQMPANAG VTVQRGGRTV AVNGLPLIDY
     TTQAHLYQAC AALAPSLAST PFAAAFAVRF ADPAFPVAAN RCAGLKARGL LSAATTAAQA
     EEALARLTAY GWEPESGALH ASLAAFEVAP SIAVTYANAL SRASVQDRLC GYSFATTSAI
     GAVQPTPAAV TNTLFATGNG IPPTAGVQLV NDRSRGVPVR DLFSSNAAGV PTWNLEGALC
     LRSLVTGTDA AARRLQSGLD ETRRTGNLQG KPAIIVHGRD DALIPVNHTS RPYAALNRRV
     EGAASRLSYI EVTNAQHFDA FIGLPATLPG YDSRYIPLHL YLNRALDAMY AHLVNGEPLP
     ASQVVRTVPR GGTPGSAPAI TAANVPPIAA MPVAADAVAI TSGAIAVPD