ECTB_NOCFA
ID ECTB_NOCFA Reviewed; 436 AA.
AC Q5YW77;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 25-MAY-2022, entry version 106.
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=NFA_27170;
OS Nocardia farcinica (strain IFM 10152).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
OX NCBI_TaxID=247156;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFM 10152;
RX PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA Shiba T., Hattori M.;
RT "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(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; AP006618; BAD57564.1; -; Genomic_DNA.
DR RefSeq; WP_011209249.1; NC_006361.1.
DR AlphaFoldDB; Q5YW77; -.
DR SMR; Q5YW77; -.
DR STRING; 247156.NFA_27170; -.
DR PRIDE; Q5YW77; -.
DR EnsemblBacteria; BAD57564; BAD57564; NFA_27170.
DR GeneID; 61133456; -.
DR KEGG; nfa:NFA_27170; -.
DR eggNOG; COG0160; Bacteria.
DR HOGENOM; CLU_016922_10_0_11; -.
DR OMA; ELDQWKP; -.
DR UniPathway; UPA00067; UER00121.
DR Proteomes; UP000006820; 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..436
FT /note="Diaminobutyrate--2-oxoglutarate transaminase"
FT /id="PRO_0000120525"
FT MOD_RES 269
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 436 AA; 46775 MW; AD91A66D6034DAD5 CRC64;
MITAETNVFE SLESNVRGYC RNWPTVFTTA KGAWLQDEDG KDYLDFFAGA GALNYGHNNP
VLKQPLIDYI ASDGITHGLD MSTAAKRKLL ETLRDTVFAP RGLDYKVQFP GPTGANAVEA
ALKLARKVTG RETVLSFTNA FHGMTLGALS VTGNAAKRAG AGVPLVHAAH MPYDGYFDNT
TADFQWMERV LDDTSSGFDR PAAVIVETVQ GEGGINVARV EWLQHLAQLC AEREILLIVD
DVQMGCGRTG PFFSFEVAGI TPDIVTLSKS IGGYGLPLAL VLFKPELDQW APGEHNGTFR
GNNPAFVTAQ VALETFWSDG ALEAATKAKG EKVATELATV AGHFPGLSTR GRGLVHGIAF
EDPSQAGKVC QVAFERGLLV ETSGSSDEVV KLLPPLTITD DELDQGLQIL TGAIDTVCTG
WGRLHHRAPA EGGERR