ID   DOEB_HALED              Reviewed;         342 AA.
AC   E1V7W0;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=N-alpha-acetyl-L-2,4-diaminobutyric acid deacetylase;
DE            Short=N-alpha-Ac-DABA;
DE            EC=3.5.1.125 {ECO:0000269|PubMed:20849449};
DE   AltName: Full=N-alpha-acetyl diaminobutyric acid deacetylase;
GN   Name=doeB {ECO:0000303|PubMed:20849449}; OrderedLocusNames=HELO_3664;
OS   Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198
OS   / 1H9).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=768066;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], FUNCTION, CATALYTIC
RP   ACTIVITY, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND NOMENCLATURE.
RC   STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9;
RX   PubMed=20849449; DOI=10.1111/j.1462-2920.2010.02336.x;
RA   Schwibbert K., Marin-Sanguino A., Bagyan I., Heidrich G., Lentzen G.,
RA   Seitz H., Rampp M., Schuster S.C., Klenk H.P., Pfeiffer F., Oesterhelt D.,
RA   Kunte H.J.;
RT   "A blueprint of ectoine metabolism from the genome of the industrial
RT   producer Halomonas elongata DSM 2581(T).";
RL   Environ. Microbiol. 13:1973-1994(2011).
CC   -!- FUNCTION: Involved in the degradation of ectoine, which allows
CC       H.elongata to utilize ectoine as both a carbon and a nitrogen source
CC       for growth. Catalyzes the deacetylation of N-alpha-acetyl-L-2,4-
CC       diaminobutyrate (N-alpha-Ac-DABA) to yield L-2,4-diaminobutyrate
CC       (DABA). {ECO:0000269|PubMed:20849449}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S)-2-acetamido-4-aminobutanoate + H2O = acetate + L-2,4-
CC         diaminobutanoate; Xref=Rhea:RHEA:40951, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:30089, ChEBI:CHEBI:58761, ChEBI:CHEBI:77587;
CC         EC=3.5.1.125; Evidence={ECO:0000269|PubMed:20849449};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40952;
CC         Evidence={ECO:0000269|PubMed:20849449};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20849449}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to grow on
CC       ectoine as carbon and nitrogen sources and accumulate N-alpha-acetyl-L-
CC       2,4-diaminobutyrate (N-alpha-Ac-DABA). {ECO:0000269|PubMed:20849449}.
CC   -!- SIMILARITY: Belongs to the DoeB deacetylase family. {ECO:0000305}.
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DR   EMBL; FN869568; CBV43548.1; -; Genomic_DNA.
DR   RefSeq; WP_013333420.1; NC_014532.2.
DR   AlphaFoldDB; E1V7W0; -.
DR   SMR; E1V7W0; -.
DR   STRING; 768066.HELO_3664; -.
DR   PRIDE; E1V7W0; -.
DR   EnsemblBacteria; CBV43548; CBV43548; HELO_3664.
DR   KEGG; hel:HELO_3664; -.
DR   eggNOG; COG3608; Bacteria.
DR   HOGENOM; CLU_035605_1_0_6; -.
DR   OMA; DAVGMYD; -.
DR   BioCyc; MetaCyc:MON-20122; -.
DR   BRENDA; 3.5.1.125; 2569.
DR   Proteomes; UP000008707; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IDA:UniProtKB.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042400; P:ectoine catabolic process; IMP:UniProtKB.
DR   InterPro; IPR007036; Aste_AspA.
DR   InterPro; IPR014336; DoeB.
DR   InterPro; IPR043795; N-alpha-Ac-DABA-like.
DR   Pfam; PF04952; AstE_AspA; 1.
DR   PIRSF; PIRSF039012; ASP; 1.
DR   TIGRFAMs; TIGR02994; ectoine_eutE; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Hydrolase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..342
FT                   /note="N-alpha-acetyl-L-2,4-diaminobutyric acid
FT                   deacetylase"
FT                   /id="PRO_0000428758"
FT   REGION          103..124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   342 AA;  36586 MW;  BB81AA20F3277667 CRC64;
     MSKQPGQQRP SPISATVDFE ADGVQHGFLK LPISNDESAW GAVMIPVTVV KRGEGPTALL
     TGGNHGDEYE GITALQKLSS RLRAEDVQGR VIIVPMMNTP ACTAGRRTSP MDGGNLNRSF
     PGDPDGSVTE KIADYFTRVL VPMSDVVLDL HSGGRTLDII PFAASHVLDD AEQQRRALEG
     AKAFGAPYAI MMFELDAEAL FDTAVERQGK IFVATELGGG GTSTPESLAI TERGIDNFLV
     HYGLVEGELQ VPDEPQIYLD MPDASCYVQS EHTGLLELTV ALGDPVTQGQ VIARVYDMTR
     SGVAPVEYRA ERDGVLAARR FPASVNMGDT IAVIAEVVES LG