DOEA_HALED
ID DOEA_HALED Reviewed; 399 AA.
AC E1V7W1;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Ectoine hydrolase;
DE EC=3.5.4.44 {ECO:0000269|PubMed:20849449};
GN Name=doeA {ECO:0000303|PubMed:20849449}; OrderedLocusNames=HELO_3665;
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, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, SUBSTRATE
RP SPECIFICITY, 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 hydrolysis of ectoine to N-acetyl-L-2,4-
CC diaminobutyric acid (N-Ac-DABA). It can produce both isoforms N-gamma-
CC acetyl-L-2,4-diaminobutyric acid (N-gamma-Ac-DABA) and N-alpha-acetyl-
CC L-2,4-diaminobutyric acid (-Nalpha-Ac-DABA), however N-alpha-Ac-DABA is
CC the essential substrate for the subsequent catabolic enzyme DoeB.
CC {ECO:0000269|PubMed:20849449}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-ectoine = (2S)-2-acetamido-4-aminobutanoate;
CC Xref=Rhea:RHEA:52304, ChEBI:CHEBI:15377, ChEBI:CHEBI:58515,
CC ChEBI:CHEBI:77587; EC=3.5.4.44;
CC Evidence={ECO:0000269|PubMed:20849449};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52305;
CC Evidence={ECO:0000269|PubMed:20849449};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20849449}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to grow on
CC ectoine as carbon source. {ECO:0000269|PubMed:20849449}.
CC -!- MISCELLANEOUS: The ectoine biosynthesis and ectoine degradation operate
CC via different isoforms of N-acetyl diamonbutyric acid: N-gamma-acetyl
CC diamonbutyric acid is the intermediate of ectoine biosynthesis and N-
CC alpha-acetyl diamonbutyric acid is the intermediate of ectoine
CC degradation. {ECO:0000305|PubMed:20849449}.
CC -!- SIMILARITY: Belongs to the peptidase M24 family. {ECO:0000305}.
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DR EMBL; FN869568; CBV43549.1; -; Genomic_DNA.
DR RefSeq; WP_013333421.1; NC_014532.2.
DR PDB; 6TWJ; X-ray; 2.15 A; A/B=2-399.
DR PDB; 6TWK; X-ray; 2.25 A; A/B=1-399.
DR PDB; 6YO9; X-ray; 2.40 A; A/B=1-399.
DR PDBsum; 6TWJ; -.
DR PDBsum; 6TWK; -.
DR PDBsum; 6YO9; -.
DR AlphaFoldDB; E1V7W1; -.
DR SMR; E1V7W1; -.
DR STRING; 768066.HELO_3665; -.
DR EnsemblBacteria; CBV43549; CBV43549; HELO_3665.
DR KEGG; hel:HELO_3665; -.
DR eggNOG; COG0006; Bacteria.
DR HOGENOM; CLU_017266_3_1_6; -.
DR OMA; PGMCFSV; -.
DR BioCyc; MetaCyc:MON-20123; -.
DR BRENDA; 3.5.4.44; 2569.
DR Proteomes; UP000008707; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016812; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides; IDA:UniProtKB.
DR GO; GO:0042400; P:ectoine catabolic process; IMP:UniProtKB.
DR Gene3D; 3.40.350.10; -; 1.
DR Gene3D; 3.90.230.10; -; 1.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000587; Creatinase_N.
DR InterPro; IPR014335; Ectoine_EutD.
DR InterPro; IPR000994; Pept_M24.
DR Pfam; PF01321; Creatinase_N; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR SUPFAM; SSF53092; SSF53092; 1.
DR SUPFAM; SSF55920; SSF55920; 1.
DR TIGRFAMs; TIGR02993; ectoine_eutD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Reference proteome.
FT CHAIN 1..399
FT /note="Ectoine hydrolase"
FT /id="PRO_0000428757"
FT HELIX 10..27
FT /evidence="ECO:0007829|PDB:6TWJ"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:6TWJ"
FT HELIX 37..44
FT /evidence="ECO:0007829|PDB:6TWJ"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:6TWJ"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:6TWJ"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:6TWJ"
FT HELIX 71..77
FT /evidence="ECO:0007829|PDB:6TWJ"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:6TWJ"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:6TWJ"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:6TWJ"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:6TWJ"
FT HELIX 103..109
FT /evidence="ECO:0007829|PDB:6TWJ"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:6TWJ"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:6TWJ"
FT HELIX 133..142
FT /evidence="ECO:0007829|PDB:6TWJ"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:6TWJ"
FT HELIX 154..158
FT /evidence="ECO:0007829|PDB:6TWJ"
FT HELIX 164..187
FT /evidence="ECO:0007829|PDB:6TWJ"
FT HELIX 194..207
FT /evidence="ECO:0007829|PDB:6TWJ"
FT HELIX 231..235
FT /evidence="ECO:0007829|PDB:6TWJ"
FT STRAND 248..260
FT /evidence="ECO:0007829|PDB:6TWJ"
FT STRAND 263..274
FT /evidence="ECO:0007829|PDB:6TWJ"
FT HELIX 278..297
FT /evidence="ECO:0007829|PDB:6TWJ"
FT HELIX 304..317
FT /evidence="ECO:0007829|PDB:6TWJ"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:6TWJ"
FT STRAND 359..362
FT /evidence="ECO:0007829|PDB:6TWJ"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:6YO9"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:6YO9"
FT STRAND 377..381
FT /evidence="ECO:0007829|PDB:6TWJ"
FT STRAND 383..390
FT /evidence="ECO:0007829|PDB:6TWJ"
FT STRAND 397..399
FT /evidence="ECO:0007829|PDB:6TWK"
SQ SEQUENCE 399 AA; 44949 MW; 9EB9D3B71FF221C7 CRC64;
MIQVSLPFTR EEYAGRLWKV RTEMASRGID VLVISDPSNM AWLTGYDGWS FYVHQCVLLG
LEGEPVWYGR RMDANGALRT CWMDPDNITY YPDHYVQNPD MHPMDYLAQT ILPDRGWHEG
VVGMEMDNYY FSAKAYQCLL RELPHARFAD ANSLVNWCRA IKSPQEIEYM RVAGKIVAGM
HSRILEVIEP GLPKSKLVSE IYRVGIEGWT SPEGKVFGGD YPAIVPMLPT GKDAAAPHLT
WDDSPFREGE GTFFEIAGVY KRYHAPMSRT VYLGRPPSEF VRAESALLEG IENGLEVAKP
GNRTADIAMA LGAAMDKYGF DRGGARCGYP IGISYPPDWG ERTMSLRPSD ETILEPGMTF
HFMPGLWVED WGLEITESIL ITESGCETLA DFPRQLFVK
