ID A0A2P8HBN2_9BACI Unreviewed; 427 AA.
AC A0A2P8HBN2;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Diaminobutyrate--2-oxoglutarate transaminase {ECO:0000256|ARBA:ARBA00014798, ECO:0000256|RuleBase:RU365034};
DE EC=2.6.1.76 {ECO:0000256|ARBA:ARBA00013155, ECO:0000256|RuleBase:RU365034};
DE AltName: Full=DABA aminotransferase {ECO:0000256|RuleBase:RU365034};
GN ORFNames=B0H94_110114 {ECO:0000313|EMBL:PSL43638.1};
OS Salsuginibacillus halophilus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Salsuginibacillus.
OX NCBI_TaxID=517424 {ECO:0000313|EMBL:PSL43638.1, ECO:0000313|Proteomes:UP000242310};
RN [1] {ECO:0000313|EMBL:PSL43638.1, ECO:0000313|Proteomes:UP000242310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.07653 {ECO:0000313|EMBL:PSL43638.1,
RC ECO:0000313|Proteomes:UP000242310};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (MAR-2018) 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|ARBA:ARBA00002189,
CC 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|ARBA:ARBA00001487,
CC 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|ARBA:ARBA00004946, ECO:0000256|RuleBase:RU365034}.
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:PSL43638.1}.
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DR EMBL; PYAV01000010; PSL43638.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8HBN2; -.
DR OrthoDB; 9807885at2; -.
DR UniPathway; UPA00067; UER00121.
DR Proteomes; UP000242310; Unassembled WGS sequence.
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:PSL43638.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000242310};
KW Transferase {ECO:0000256|RuleBase:RU365034, ECO:0000313|EMBL:PSL43638.1}.
SQ SEQUENCE 427 AA; 46774 MW; 47B67FD1DBDCDFAE CRC64;
MNFNDLSIFE NLESEVRSYC RGFPAVFHKA KDHKLWDLDG NEYVDFFSGA GALNYGHNNE
KMKQALIQYL TEDGITHSLD MASKAKAEFL QSFNDIILKP RNLDYKTMFP GPTGTNTVES
ALKLARKVTG RTNVISFTNG FHGMTIGALS VTGNAFKRQG AGIPLNHSVT MPYDAYNGDT
KAQLDYVKQF IDDNGSGVDM PAAFILETVQ GEGGLNAASN EWLQGIEKIC RERGILLIID
DVQAGVGRTG TFFSFEPAGI NPDIVCLSKS IGGYGLPLAL TLIKPEYDIW APGEHNGTFR
GNNPAFVAAT AALEYWKDDT LEKSVQEKSK KITNFLQDMT KKYPELRGSL KGRGFMQGIA
CDVEGLAEDV AEKAFEKGLI METAGAEDEV FKLFPPITID DAGLEDGLNR LEAAIEATVK
QKDLVTS
//
