ID M1P3B8_9CORY Unreviewed; 419 AA.
AC M1P3B8;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Diaminobutyrate--2-oxoglutarate aminotransferase {ECO:0000313|EMBL:AGF71181.1};
DE EC=2.6.1.76 {ECO:0000313|EMBL:AGF71181.1};
GN ORFNames=A605_00825 {ECO:0000313|EMBL:AGF71181.1};
OS Corynebacterium halotolerans YIM 70093 = DSM 44683.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1121362 {ECO:0000313|EMBL:AGF71181.1, ECO:0000313|Proteomes:UP000011723};
RN [1] {ECO:0000313|EMBL:AGF71181.1, ECO:0000313|Proteomes:UP000011723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 70093 {ECO:0000313|EMBL:AGF71181.1};
RX PubMed=23408721;
RA Ruckert C., Albersmeier A., Al-Dilaimi A., Niehaus K., Szczepanowski R.,
RA Kalinowski J.;
RT "Genome sequence of the halotolerant bacterium Corynebacterium halotolerans
RT type strain YIM 70093(T) (= DSM 44683(T)).";
RL Stand. Genomic Sci. 7:284-293(2012).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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; CP003697; AGF71181.1; -; Genomic_DNA.
DR RefSeq; WP_015399605.1; NZ_JIAJ01000002.1.
DR AlphaFoldDB; M1P3B8; -.
DR STRING; 1121362.A605_00825; -.
DR KEGG; chn:A605_00825; -.
DR PATRIC; fig|1121362.3.peg.156; -.
DR eggNOG; COG0160; Bacteria.
DR HOGENOM; CLU_016922_10_0_11; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000011723; Chromosome.
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:0009058; P:biosynthetic process; IEA:InterPro.
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: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:0000313|EMBL:AGF71181.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000011723};
KW Transferase {ECO:0000313|EMBL:AGF71181.1}.
SQ SEQUENCE 419 AA; 45194 MW; B62BC244305492BA CRC64;
MDTTIFEHHE SSIRGYCRNF PTVFASASNA RQTAEDGTSY IDFFSGAGVL NFGHNNPRMK
EAMIEFLQSD GVAHSLDTYT TTKRDFIQRF HEVVLAPRGM DHRLQFMGPT GSNAVEAALK
LARLSTGRRE IVAFSHGFHG MTLGSLAATA NHAFRQWAGV PLTDVVRLPF ETAPGGRTAI
AEYAASLRDT SSGNTPPAAF LVEPVQAEGG VNVASREWLH EVQDLAREVG ALFIIDDIQA
GIGRTGSYFS FDDMDLDPDI ITLAKGLGGF GTPIAMNLNK PAVDDNWSPG AHTGTFRGQG
LSFIAGTVAL GYFTDEAFLA GVRDKGQVMR ERLERIAADH PDRDWEVRGR GMMQALDTGD
GAFAKQVQAE AFDRGLLIGP CGTGGQVIKL IPPLTIGEDD LAEGLDLFEQ AIRAAQAVT
//
