ID D8K6D7_NITWC Unreviewed; 433 AA.
AC D8K6D7;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Diaminobutyrate--2-oxoglutarate transaminase {ECO:0000256|RuleBase:RU365034};
DE EC=2.6.1.76 {ECO:0000256|RuleBase:RU365034};
DE AltName: Full=DABA aminotransferase {ECO:0000256|RuleBase:RU365034};
GN OrderedLocusNames=Nwat_1572 {ECO:0000313|EMBL:ADJ28464.1};
OS Nitrosococcus watsoni (strain C-113).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Nitrosococcus.
OX NCBI_TaxID=105559 {ECO:0000313|EMBL:ADJ28464.1, ECO:0000313|Proteomes:UP000000393};
RN [1] {ECO:0000313|EMBL:ADJ28464.1, ECO:0000313|Proteomes:UP000000393}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C-113 {ECO:0000313|EMBL:ADJ28464.1,
RC ECO:0000313|Proteomes:UP000000393};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Malfatti S.A., Chain P.S.G., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Cambell M.A., Heidelberg J.F., Klotz M.G., Woyke T.;
RT "Complete sequence of chromosome of Nitrosococcus watsoni C-113.";
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU365034}.
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|RuleBase:RU365034};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU365034};
CC -!- PATHWAY: Amine and polyamine biosynthesis; ectoine biosynthesis; L-
CC ectoine from L-aspartate 4-semialdehyde: step 1/3.
CC {ECO:0000256|RuleBase:RU365034}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR EMBL; CP002086; ADJ28464.1; -; Genomic_DNA.
DR RefSeq; WP_013220556.1; NC_014315.1.
DR AlphaFoldDB; D8K6D7; -.
DR STRING; 105559.Nwat_1572; -.
DR KEGG; nwa:Nwat_1572; -.
DR eggNOG; COG0160; Bacteria.
DR HOGENOM; CLU_016922_10_0_6; -.
DR OrthoDB; 9770449at2; -.
DR UniPathway; UPA00067; UER00121.
DR Proteomes; UP000000393; 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; 3.90.1150.10; 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; IPR012773; Ectoine_EctB.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR00709; dat; 1.
DR NCBIfam; TIGR02407; ectoine_ectB; 1.
DR PANTHER; PTHR43552; DIAMINOBUTYRATE--2-OXOGLUTARATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR43552:SF2; DIAMINOBUTYRATE--2-OXOGLUTARATE TRANSAMINASE; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 3.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|RuleBase:RU365034,
KW ECO:0000313|EMBL:ADJ28464.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Transferase {ECO:0000256|RuleBase:RU365034, ECO:0000313|EMBL:ADJ28464.1}.
SQ SEQUENCE 433 AA; 48075 MW; B48FB8B029AFD05D CRC64;
MRIIEQLESE VRGYVRSFPV VFDTAKGSYL YDEQGNEYID FFSGAGTLNY GHNNPIISKA
LLKYIERDGI IHGLDKATVA KVAFLQKFYD TILSPRNLEY KVQFTGPTGT NATETALKLA
RMIKRRSNVI AFTNGYHGLT MGSLAVTGNT FYRDESYGVR NNSAFMPYDG YFGPDVDTIE
YFRRFLEDSS SGVDLPAAVI LETVQAEGGI NVASDEWLRR LERLCREFDI LLIVDDIQVG
NGRTGTFFSF ERAGITPDMV TLSKSIGGGL PLSLLLMRPE LDQWKPGEHT GTFRGNNLAF
VAAVESLSAY WENDDLTEAV KYKGEIIETE LKAIAEKYPE LNGKVRGVGM VWGLEMPRNG
FTSQVSKEAF ENGVIIEIAG ADDQVLKFLP SLTIEETILR EGLGIIDKAI GNLLARKREM
RSGNTQPLAA EAV
//
