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Database: UniProt
Entry: Q7N1D8_PHOLL
LinkDB: Q7N1D8_PHOLL
Original site: Q7N1D8_PHOLL 
ID   Q7N1D8_PHOLL            Unreviewed;       436 AA.
AC   Q7N1D8;
DT   15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2003, sequence version 1.
DT   24-JAN-2024, entry version 104.
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=plu3538 {ECO:0000313|EMBL:CAE15911.1};
OS   Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS   TT01) (Photorhabdus luminescens subsp. laumondii).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Photorhabdus.
OX   NCBI_TaxID=243265 {ECO:0000313|EMBL:CAE15911.1, ECO:0000313|Proteomes:UP000002514};
RN   [1] {ECO:0000313|Proteomes:UP000002514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15139 / CIP 105565 / TT01
RC   {ECO:0000313|Proteomes:UP000002514};
RX   PubMed=14528314; DOI=10.1038/nbt886;
RA   Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA   Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA   Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA   Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA   Glaser P., Boemare N., Danchin A., Kunst F.;
RT   "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT   luminescens.";
RL   Nat. Biotechnol. 21:1307-1313(2003).
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; BX571870; CAE15911.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7N1D8; -.
DR   STRING; 243265.plu3538; -.
DR   KEGG; plu:plu3538; -.
DR   eggNOG; COG0160; Bacteria.
DR   HOGENOM; CLU_016922_10_0_6; -.
DR   OMA; YESKARS; -.
DR   UniPathway; UPA00067; UER00121.
DR   Proteomes; UP000002514; 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; 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   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   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002514};
KW   Transferase {ECO:0000256|RuleBase:RU365034}.
SQ   SEQUENCE   436 AA;  48856 MW;  BD4AA9089D74A221 CRC64;
     MEIDEIFNNY ESKARSYCRR FPVIFRNGIG STLIDIDGKS YIDFLCGAGA LNYGHNNTII
     KQQIFKYIQD DGIIMGLDLY SEAKMEFIST FVDKILKPRQ LEYRLQFTSP TGTSVIESAV
     KLARKYTKRE NIVCFTNAFH GMTGVSLSLT GSQHHRQPGL YSQITRLPFD GYIDGEFDYI
     GYFRKLLTDS SSGVDLPAAV ILETVQGEGG LNVASVEWLR ALRKLTQEFN ILLIVDDIQS
     GCGRTGTFFS FERASIKPDL VCLSKSIGGI GLPMSLLLIS PDIDVWKPAE DNGTFRGNNL
     AFVASKAMLN EYWGDSSFQK IIEHKAELIR AYLDSLAKEY HEFVLRVKGI GFMQGIEMVD
     SSLTQYLVKH CFENGLIVEL CGPNDEVLKL MPALTIDEDT LVKGLRIIEQ ALASLKSRNS
     NNCESEFQRV SASSNY
//
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