ID Q0A9E7_ALKEH Unreviewed; 440 AA.
AC Q0A9E7;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 91.
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=Mlg_1191 {ECO:0000313|EMBL:ABI56540.1};
OS Alkalilimnicola ehrlichii (strain ATCC BAA-1101 / DSM 17681 / MLHE-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Alkalilimnicola.
OX NCBI_TaxID=187272 {ECO:0000313|EMBL:ABI56540.1, ECO:0000313|Proteomes:UP000001962};
RN [1] {ECO:0000313|Proteomes:UP000001962}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1101 / DSM 17681 / MLHE-1
RC {ECO:0000313|Proteomes:UP000001962};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Oremland R.S.,
RA Hoeft S.E., Switzer-Blum J., Kulp T., King G., Tabita R., Witte B.,
RA Santini J.M., Basu P., Hollibaugh J.T., Xie G., Stolz J.F., Richardson P.;
RT "Complete sequence of Alkalilimnicola ehrilichei MLHE-1.";
RL Submitted (AUG-2006) 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; CP000453; ABI56540.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0A9E7; -.
DR KEGG; aeh:Mlg_1191; -.
DR eggNOG; COG0160; Bacteria.
DR HOGENOM; CLU_016922_10_0_6; -.
DR UniPathway; UPA00067; UER00121.
DR Proteomes; UP000001962; 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; 2.
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:ABI56540.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000001962};
KW Transferase {ECO:0000256|RuleBase:RU365034, ECO:0000313|EMBL:ABI56540.1}.
SQ SEQUENCE 440 AA; 48694 MW; 1D9BAEE436FD4459 CRC64;
MTIDYMHTIE EHESIVRSYV RSFPTVFDTA KGSYLYNLDG EAYLDFFAGA SVMNYGHNHP
EIKKALIEYL ERDGVTHSLD MASKARAEFL DTFHRLILEP RGMDYRVQFP GPTGTNAVET
ALKIARKVTG REDVISFTNA FHGMTLGSLS VTGNEFKRKG AGIPLTHGQT MPYCGYFGPC
VNRGGSERNC VDYLDRMLKD GGSGVDHPAA IIMEPIQGEG GLNVACAEWM RQVEALCKKY
DMLLIVDDIQ AGNGRAGSYF SFEESGIKPD VVTVSKSLSG YGMPLSITLV KPEHDIWEPG
EHNGTFRGFN PAVVTAKRAL ELFWSDDSFQ KEVLRKGEKM REFLAGLLKK YPQAPGQVRG
RGMMQGIAFD NAELAEKISE HAFQRKLIIE TSGPRDEVLK LLPPLVTSDE DLEKGLAIIE
QALVAAMEEL GMNRDAASSQ
//
