(data stored in SCRATCH zone)

SWISSPROT: A4F709_SACEN

ID   A4F709_SACEN            Unreviewed;       415 AA.
AC   A4F709;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 75.
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   Name=ectB {ECO:0000313|EMBL:CAL99833.1};
GN   OrderedLocusNames=SACE_0484 {ECO:0000313|EMBL:CAL99833.1};
GN   ORFNames=A8924_0882 {ECO:0000313|EMBL:PFG93632.1};
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748
OS   / NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948 {ECO:0000313|EMBL:CAL99833.1, ECO:0000313|Proteomes:UP000006728};
RN   [1] {ECO:0000313|EMBL:CAL99833.1, ECO:0000313|Proteomes:UP000006728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC   NRRL 2338 {ECO:0000313|Proteomes:UP000006728}, and NRRL 2338
RC   {ECO:0000313|EMBL:CAL99833.1};
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N.,
RA   Dickens S., Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
RN   [2] {ECO:0000313|EMBL:PFG93632.1, ECO:0000313|Proteomes:UP000225825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40517 {ECO:0000313|EMBL:PFG93632.1,
RC   ECO:0000313|Proteomes:UP000225825};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes reversively the conversion of L-aspartate
CC       beta-semialdehyde (ASA) to L-2,4-diaminobutyrate (DABA) by
CC       transamination 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,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:58761,
CC         ChEBI:CHEBI:537519; EC=2.6.1.76;
CC         Evidence={ECO:0000256|RuleBase:RU365034};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|RuleBase:RU365034};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; ectoine biosynthesis;
CC       L-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; AM420293; CAL99833.1; -; Genomic_DNA.
DR   EMBL; PDBV01000001; PFG93632.1; -; Genomic_DNA.
DR   RefSeq; WP_009947388.1; NZ_PDBV01000001.1.
DR   STRING; 405948.SACE_0484; -.
DR   EnsemblBacteria; CAL99833; CAL99833; SACE_0484.
DR   KEGG; sen:SACE_0484; -.
DR   eggNOG; ENOG4108JPW; Bacteria.
DR   eggNOG; COG0160; LUCA.
DR   HOGENOM; HOG000020206; -.
DR   KO; K00836; -.
DR   OMA; NLMPGVQ; -.
DR   OrthoDB; 386839at2; -.
DR   BioCyc; SERY405948:SACE_RS02390-MONOMER; -.
DR   UniPathway; UPA00067; UER00121.
DR   Proteomes; UP000006728; Chromosome.
DR   Proteomes; UP000225825; 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; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR004637; Dat.
DR   InterPro; IPR012773; Ectoine_EctB.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR43552; PTHR43552; 1.
DR   PANTHER; PTHR43552:SF2; PTHR43552:SF2; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 3.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR00709; dat; 1.
DR   TIGRFAMs; TIGR02407; ectoine_ectB; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; A4F709.
DR   SWISS-2DPAGE; A4F709.
KW   Aminotransferase {ECO:0000256|RuleBase:RU365034,
KW   ECO:0000313|EMBL:CAL99833.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006728,
KW   ECO:0000313|Proteomes:UP000225825};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560};
KW   Pyruvate {ECO:0000313|EMBL:CAL99833.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006728};
KW   Transferase {ECO:0000256|RuleBase:RU365034,
KW   ECO:0000313|EMBL:CAL99833.1}.
SQ   SEQUENCE   415 AA;  45486 MW;  442F3B83D8815C80 CRC64;
     MNNIFESLES EVRSYCRTWP AVFDVAKGSY LYAEDGTAYL DFFAGAGALN YGHNNPVLKR
     KLLEYLERDG VTHGLDQATK AKREFLETLD EKLLKPRGLD YKVQFPGPTG TNSVESALKL
     VRKITGRESI ISFTNAFHGM TLGSLSVTGN SMKRGGAGIP LVHATPMPYD DYFDGQVPDF
     LYFERMLEDS GSGLNEPAAV IVETLQGEGG INSSRPEWLR GLYELCQKHG ILMIVDDVQM
     GCGRTGPFFS FEEAGIQPDI VCLSKSIGGY GMPLALTLIK SEHDVWDPGE HNGTFRGNNP
     AFVTATEALK EYWSDDRLEK STIAKGERVG EVLDELVAKY DGALAKGRGL ARGLGFEDPE
     IAGKVSKAAF DRKLILETSG PDSEVIKIMP PLTVSDEELE QGLQIIRESV HSVLA
//

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