(data stored in ACNUC1104 zone)

SWISSPROT: A4F708_SACEN

ID   A4F708_SACEN            Unreviewed;       133 AA.
AC   A4F708;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 55.
DE   RecName: Full=L-2,4-diaminobutyric acid acetyltransferase {ECO:0000256|RuleBase:RU365045};
DE            Short=DABA acetyltransferase {ECO:0000256|RuleBase:RU365045};
DE            EC=2.3.1.178 {ECO:0000256|RuleBase:RU365045};
GN   Name=ectA {ECO:0000256|RuleBase:RU365045,
GN   ECO:0000313|EMBL:CAL99832.1};
GN   OrderedLocusNames=SACE_0483 {ECO:0000313|EMBL:CAL99832.1};
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:CAL99832.1, ECO:0000313|Proteomes:UP000006728};
RN   [1] {ECO:0000313|EMBL:CAL99832.1, 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};
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).
CC   -!- FUNCTION: Catalyzes the acetylation of L-2,4-diaminobutyrate
CC       (DABA) to gamma-N-acetyl-alpha,gamma-diaminobutyric acid (ADABA)
CC       with acetyl coenzyme A. {ECO:0000256|RuleBase:RU365045}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + L-2,4-diaminobutanoate = (2S)-4-acetamido-2-
CC         aminobutanoate + CoA + H(+); Xref=Rhea:RHEA:16901,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:58761, ChEBI:CHEBI:58929; EC=2.3.1.178;
CC         Evidence={ECO:0000256|RuleBase:RU365045};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; ectoine biosynthesis;
CC       L-ectoine from L-aspartate 4-semialdehyde: step 2/3.
CC       {ECO:0000256|RuleBase:RU365045}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. EctA
CC       subfamily. {ECO:0000256|RuleBase:RU365045}.
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DR   EMBL; AM420293; CAL99832.1; -; Genomic_DNA.
DR   STRING; 405948.SACE_0483; -.
DR   EnsemblBacteria; CAL99832; CAL99832; SACE_0483.
DR   KEGG; sen:SACE_0483; -.
DR   eggNOG; ENOG4108Z24; Bacteria.
DR   eggNOG; ENOG4111N89; LUCA.
DR   HOGENOM; HOG000078070; -.
DR   KO; K06718; -.
DR   OMA; YAYLLWC; -.
DR   UniPathway; UPA00067; UER00122.
DR   Proteomes; UP000006728; Chromosome.
DR   GO; GO:0033816; F:diaminobutyrate acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019491; P:ectoine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR017255; AcTrfase_GNAT_prd.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR012772; Ectoine_EctA.
DR   InterPro; IPR000182; GNAT_dom.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   PIRSF; PIRSF037663; Acetyltransf_GNAT_prd; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   TIGRFAMs; TIGR02406; ectoine_EctA; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
DR   PRODOM; A4F708.
DR   SWISS-2DPAGE; A4F708.
KW   Acyltransferase {ECO:0000256|RuleBase:RU365045};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006728};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006728};
KW   Transferase {ECO:0000256|RuleBase:RU365045,
KW   ECO:0000313|EMBL:CAL99832.1}.
FT   DOMAIN        1    120       N-acetyltransferase.
FT                                {ECO:0000259|PROSITE:PS51186}.
SQ   SEQUENCE   133 AA;  14075 MW;  EC1AB5511C88E2E2 CRC64;
     MWCRDFAQTS AVARVDGEVV GFVTGFIRPD ASDTIVVWQI AVDASQRGGG VAGKLLSHLL
     DRVVPRGVRY LETTITPDNT ASIKLFSALA RDRGAELVSS ELFTAELFPD AHLGEDLYRI
     GPFAAAPAAA GGA
//

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