ECTB_STRAQ
ID ECTB_STRAQ Reviewed; 420 AA.
AC Q6QUY9;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 67.
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; Synonyms=thpB;
OS Streptomyces anulatus (Streptomyces chrysomallus).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1892;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 11523 / DSM 40128 / JCM 4296 / LMG 20459 / NBRC 15393;
RX PubMed=15128576; DOI=10.1128/aem.70.5.3130-3132.2004;
RA Prabhu J., Schauwecker F., Grammel N., Keller U., Bernhard M.;
RT "Functional expression of the ectoine hydroxylase gene (thpD) from
RT Streptomyces chrysomallus in Halomonas elongata.";
RL Appl. Environ. Microbiol. 70:3130-3132(2004).
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; AY524544; AAS02095.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6QUY9; -.
DR SMR; Q6QUY9; -.
DR PRIDE; Q6QUY9; -.
DR UniPathway; UPA00067; UER00121.
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; Transferase.
FT CHAIN 1..420
FT /note="Diaminobutyrate--2-oxoglutarate transaminase"
FT /id="PRO_0000120528"
FT MOD_RES 271
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 420 AA; 45883 MW; 89785F9C8AA7791A CRC64;
MTITPPALSV FETLESEVRS YCRGWPAVFD RAQGARLTDE DGHSYLDFFA GAGSLNYGHN
NPVLKRALID YIERDGITHG LDMATTAKRA FLETFQNVIL RPRDLPYKVM FPGPTGTNAV
ESALKLARKV KGRESVVSFT NAFHGMSLGS LAVTGNAFKR AGAGIPLVHG TPMPFDNYFD
GTVPDFLWFE RLLEDQGSGL NKPAAVIVET VQGEGGINVA RAEWLRALQE LCLRQVMLLI
VDDIQMGCGR TGGFFSFEEA GIVPDIVTLS KSISGYGLPM SLCLFKPELD IWEPGEHNGT
FRGNNPAFVT AAAVLDAYWA DGQMEKQTLA RGEQVEQTLL AICAEEPTAQ FRGRGLVWGM
EFEDKARASA VCARAFELGL LLETSGPQSE VVKLLPPLTI TPEELDEGLR TLARCVRETA
