ECTB_SPOPA
ID ECTB_SPOPA Reviewed; 426 AA.
AC Q9AP34;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 79.
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;
OS Sporosarcina pasteurii (Bacillus pasteurii).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX NCBI_TaxID=1474;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TRANSCRIPTIONAL REGULATION.
RC STRAIN=ATCC 11859 / DSM 33 / NCIB 8841 / NCTC 4822;
RX PubMed=11823218; DOI=10.1128/aem.68.2.772-783.2002;
RA Kuhlmann A.U., Bremer E.;
RT "Osmotically regulated synthesis of the compatible solute ectoine in
RT Bacillus pasteurii and related Bacillus spp.";
RL Appl. Environ. Microbiol. 68:772-783(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:0000305}.
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 -!- INDUCTION: By osmotic stress. {ECO:0000269|PubMed:11823218}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF316874; AAK12084.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9AP34; -.
DR SMR; Q9AP34; -.
DR PRIDE; Q9AP34; -.
DR KEGG; ag:AAK12084; -.
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 2: Evidence at transcript level;
KW Aminotransferase; Pyridoxal phosphate; Stress response; Transferase.
FT CHAIN 1..426
FT /note="Diaminobutyrate--2-oxoglutarate transaminase"
FT /id="PRO_0000120518"
FT MOD_RES 272
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 426 AA; 46844 MW; 32249A9D81E79E1A CRC64;
MLLTKEKNGM EIIEERESAV RSYSRSFPTV FEKAKDHLVW DVDGKEYIDF FAGAGSLNYG
HNNEKMKTKI MDYVMNDGIS HSLDMGTVAR AEFLETFNEV ILRPRNLDYK VMFPGPTGTN
TVESALKIAR KVTGRQNIIS FTNAFHGMTL GSLSISGNSS IRNGAGVPLT NTISMPYDTF
FKNGNAIDYL EQYLEDTGSG VDLPAAMILE TVQGEGGINA ASFEWLRGIE KLCRRYDILL
IIDDVQAGCG RTGTFFSFEP AGIQPDIVCL SKSIGGYGLP LAITLIKPEH DIWEPGEHNG
TFRGNNMAIV AATEALSYWK TDDLAKSVQK KSKIIKLRFE QIVEDYPELK ATTRGRGFMQ
GIACGKGKEA YATKICAKAF EKGVIMETSG PSGEVVKFLG ALTIDETSLI KGLGILEEAT
EEVVRQ
