ID   DOED_HALED              Reviewed;         469 AA.
AC   E1V7V7;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Diaminobutyrate--2-oxoglutarate transaminase;
DE            EC=2.6.1.76 {ECO:0000305|PubMed:20849449};
DE   AltName: Full=Diaminobutyric acid transaminase {ECO:0000303|PubMed:20849449};
GN   Name=doeD {ECO:0000303|PubMed:20849449}; OrderedLocusNames=HELO_3661;
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, AND DISRUPTION
RP   PHENOTYPE.
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. Probably catalyzes the conversion of L-2,4-diaminobutyrate
CC       (DABA) to L-aspartate beta-semialdehyde (ASA) by transamination with 2-
CC       oxoglutarate. {ECO:0000269|PubMed:20849449}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-2,4-diaminobutanoate = L-aspartate 4-
CC         semialdehyde + L-glutamate; Xref=Rhea:RHEA:11160, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:58761, ChEBI:CHEBI:537519;
CC         EC=2.6.1.76; Evidence={ECO:0000305|PubMed:20849449};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11161;
CC         Evidence={ECO:0000305|PubMed:20849449};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Deletion mutant is impaired in growth on ectoine
CC       as a sole carbon source. {ECO:0000269|PubMed:20849449}.
CC   -!- MISCELLANEOUS: DoeD and EctB both catalyze the same transamination
CC       reaction between L-aspartate 4-semialdehyde and L-2,4-diaminobutanoate
CC       coupled to the 2-oxoglutarate/L-glutamate pair. This reversible
CC       reaction is part of both, ectoine biosynthesis and ectoine degradation.
CC       {ECO:0000305|PubMed:20849449}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; FN869568; CBV43545.1; -; Genomic_DNA.
DR   RefSeq; WP_013333417.1; NC_014532.2.
DR   AlphaFoldDB; E1V7V7; -.
DR   SMR; E1V7V7; -.
DR   STRING; 768066.HELO_3661; -.
DR   EnsemblBacteria; CBV43545; CBV43545; HELO_3661.
DR   KEGG; hel:HELO_3661; -.
DR   eggNOG; COG0161; Bacteria.
DR   HOGENOM; CLU_016922_4_1_6; -.
DR   OMA; HCMEYRK; -.
DR   BioCyc; MetaCyc:MON-20120; -.
DR   Proteomes; UP000008707; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0045303; F:diaminobutyrate-2-oxoglutarate transaminase activity; IDA:UniProtKB.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0042400; P:ectoine catabolic process; IMP:UniProtKB.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase; Cytoplasm; Pyridoxal phosphate; Reference proteome;
KW   Transferase.
FT   CHAIN           1..469
FT                   /note="Diaminobutyrate--2-oxoglutarate transaminase"
FT                   /id="PRO_0000428759"
FT   MOD_RES         290
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   469 AA;  50881 MW;  16186F4252909700 CRC64;
     MTTHKDLIDR DRKVTFHAST HLRDFAHGDA PGRVITGGKG IKIVDKDGRE FIDGFAGLYC
     VNIGYGRSEV AEAIYQQALE MSYYHTYVGH SNEPQIALSE KILELAGPGM SKVYYGMSGS
     DANETQLKIV RYYNNVLGRP QKKKVISRMR GYHGSGIASG SLTGLKAFHD HFDLPIETIR
     HTEAPYYYHR AAEQEGMTER EFSKHCAAKL EEMILAEGPD TVAAFIGEPV LGTGGIVPPP
     EGYWDEIQAV LTKYDVLLIA DEVVCGFGRT GSDFGSHHYG IKPDLITIAK GLTSAYQPLS
     GVIVGDRVWE VLEQGTGEYG PIGHGWTYSG HALGCAAGLA NLAIIEREGL TANAAETGAY
     LQERMKAAFA DHPVVGQVRG VGMMAALEFS VDPAARRHFD PSLKVGPRMS AAALEEDLIA
     RAMPQGDILG FAPPLTTTRE EVDEIVARTE RAVNKVTDAL TREGAIQAA