ID V9GC60_9BACL Unreviewed; 322 AA.
AC V9GC60;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Diaminobutyrate--2-oxoglutarate transaminase {ECO:0000256|ARBA:ARBA00014798};
DE EC=2.6.1.76 {ECO:0000256|ARBA:ARBA00013155};
DE AltName: Full=DABA aminotransferase {ECO:0000256|ARBA:ARBA00030665};
DE AltName: Full=Diaminobutyrate--2-oxoglutarate aminotransferase {ECO:0000256|ARBA:ARBA00031476};
DE AltName: Full=L-2,4-diaminobutyric acid transaminase {ECO:0000256|ARBA:ARBA00029744};
GN ORFNames=JCM10914_2627 {ECO:0000313|EMBL:GAE06464.1};
OS Paenibacillus sp. JCM 10914.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1236974 {ECO:0000313|EMBL:GAE06464.1, ECO:0000313|Proteomes:UP000018028};
RN [1] {ECO:0000313|EMBL:GAE06464.1, ECO:0000313|Proteomes:UP000018028}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10914 {ECO:0000313|EMBL:GAE06464.1,
RC ECO:0000313|Proteomes:UP000018028};
RA Ohkuma M., Yuki M., Oshima K., Suda W., Oshida Y., Kitamura K., Iida T.,
RA Hattori M.;
RT "Draft Genome Sequence of the Alkaliphilic and Xylanolytic Paenibacillus
RT sp. Strain JCM 10914, Isolated from the Gut of a Soil-Feeding Termite.";
RL Genome Announc. 2:e01144-13(2014).
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:0000256|ARBA:ARBA00002189}.
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:0000256|ARBA:ARBA00001487};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- PATHWAY: Amine and polyamine biosynthesis; ectoine biosynthesis; L-
CC ectoine from L-aspartate 4-semialdehyde: step 1/3.
CC {ECO:0000256|ARBA:ARBA00004946}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAE06464.1}.
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DR EMBL; BAUO01000007; GAE06464.1; -; Genomic_DNA.
DR AlphaFoldDB; V9GC60; -.
DR STRING; 1236974.GCA_001315105_02548; -.
DR UniPathway; UPA00067; UER00121.
DR Proteomes; UP000018028; Unassembled WGS sequence.
DR GO; GO:0045303; F:diaminobutyrate-2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR004637; Dat.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43552; DIAMINOBUTYRATE--2-OXOGLUTARATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR43552:SF1; DIAMINOBUTYRATE--2-OXOGLUTARATE AMINOTRANSFERASE; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:GAE06464.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000018028};
KW Transferase {ECO:0000313|EMBL:GAE06464.1}.
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 322 AA; 34873 MW; E41D4DEBEE200E2F CRC64;
MHHVTATAEV SANSRYLRSQ QERESSARSY PRRIPIAIAE AEGIYVRDMD GKVYYDCLSG
AGTLALGHNH PVVITAIREL LDQKAPLHTL DLTTPLKESF VDELFASLPP SFASRARIQF
CGPTGGDAVE ASIKLMKTAT GRRSVLAFHG GYHGSTHAAM SLSGTLGQKE RVNGLMPDVH
YLPYPYTFRC PFGSGGAETE RLSLNYIENV LRDPESGIVP PAAVIVEPVQ GEGGSIPASA
NWLRELRRIT KERDIPLILD EVQTGLGRTG KLFAFEHADI VPDALILSKA IGGSCRCRSY
YTTNATTYGN LVRISAPSAA TS
//
