ECTB_OCEIH
ID ECTB_OCEIH Reviewed; 426 AA.
AC Q8ESU8;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Diaminobutyrate--2-oxoglutarate transaminase;
DE EC=2.6.1.76;
DE AltName: Full=DABA aminotransferase;
DE AltName: Full=Diaminobutyrate--2-oxoglutarate aminotransferase;
DE AltName: Full=L-2,4-diaminobutyric acid transaminase;
GN Name=ectB; OrderedLocusNames=OB0518;
OS Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS 3954 / HTE831).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=221109;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX PubMed=12235376; DOI=10.1093/nar/gkf526;
RA Takami H., Takaki Y., Uchiyama I.;
RT "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT and its unexpected adaptive capabilities to extreme environments.";
RL Nucleic Acids Res. 30:3927-3935(2002).
CC -!- FUNCTION: Catalyzes reversively the conversion of L-aspartate beta-
CC semialdehyde (ASA) to L-2,4-diaminobutyrate (DABA) by transamination
CC with L-glutamate. {ECO:0000250}.
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;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Amine and polyamine biosynthesis; ectoine biosynthesis; L-
CC ectoine from L-aspartate 4-semialdehyde: step 1/3.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; BA000028; BAC12474.1; -; Genomic_DNA.
DR RefSeq; WP_011064921.1; NC_004193.1.
DR AlphaFoldDB; Q8ESU8; -.
DR SMR; Q8ESU8; -.
DR STRING; 221109.22776197; -.
DR EnsemblBacteria; BAC12474; BAC12474; BAC12474.
DR KEGG; oih:OB0518; -.
DR eggNOG; COG0160; Bacteria.
DR HOGENOM; CLU_016922_10_0_9; -.
DR OMA; ELDQWKP; -.
DR OrthoDB; 386839at2; -.
DR PhylomeDB; Q8ESU8; -.
DR UniPathway; UPA00067; UER00121.
DR Proteomes; UP000000822; Chromosome.
DR GO; GO:0045303; F:diaminobutyrate-2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0047307; F:diaminobutyrate-pyruvate transaminase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019491; P:ectoine biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR004637; Dat.
DR InterPro; IPR012773; Ectoine_EctB.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43552; PTHR43552; 1.
DR PANTHER; PTHR43552:SF2; PTHR43552:SF2; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR00709; dat; 1.
DR TIGRFAMs; TIGR02407; ectoine_ectB; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..426
FT /note="Diaminobutyrate--2-oxoglutarate transaminase"
FT /id="PRO_0000120526"
FT MOD_RES 274
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 426 AA; 46943 MW; B966DCD55EB776DC CRC64;
MTTIVDKARN DMAVFEEMES AVRSYSRGWP VVFEKAKGYK LWDKNGNEYI DFFAGAGALN
YGHNPSEMQK VMIDYIQNDG VIHSLDMATA PRKKFLESFN EIILKPRNMD YKVMFPGPTG
TNTVESALKI ARKVTGRDTV IGFTNAFHGM TIGSLSVTGN SFKRNGAGIP LNHAISMPFD
QYVDEQDSIA YIERFLEDSG SGVALPAAFI LETVQGEGGI NAARLEWVKK IEEICRKWDI
LLIIDDVQAG CGRTGTFFSF EEAGINPDIV CLSKSIGGVG LPMAITLIKP EFDQWGPGEH
NGTFRGNNLA FLAATEALNN WKTDAFSQNI KKMSSLFQER MKRIVEKFPE LNADLRGRGL
MLGIGVHVDG LAGEICAEAF SRGLILETSG AKDEVVKFLP PLIIDEDGIE KGMDILEESI
QAALEK