(data stored in SCRATCH zone)

SWISSPROT: Q47T79_THEFY

ID   Q47T79_THEFY            Unreviewed;       190 AA.
AC   Q47T79;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 80.
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   OrderedLocusNames=Tfu_0300 {ECO:0000313|EMBL:AAZ54338.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54338.1, ECO:0000313|Proteomes:UP000000434};
RN   [1] {ECO:0000313|Proteomes:UP000000434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX {ECO:0000313|Proteomes:UP000000434};
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(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; CP000088; AAZ54338.1; -; Genomic_DNA.
DR   STRING; 269800.Tfu_0300; -.
DR   EnsemblBacteria; AAZ54338; AAZ54338; Tfu_0300.
DR   KEGG; tfu:Tfu_0300; -.
DR   eggNOG; ENOG4108Z24; Bacteria.
DR   eggNOG; ENOG4111N89; LUCA.
DR   HOGENOM; HOG000078070; -.
DR   KO; K06718; -.
DR   OMA; YAYLLWC; -.
DR   UniPathway; UPA00067; UER00122.
DR   Proteomes; UP000000434; 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; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR012772; Ectoine_EctA.
DR   InterPro; IPR000182; GNAT_dom.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   TIGRFAMs; TIGR02406; ectoine_EctA; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q47T79.
DR   SWISS-2DPAGE; Q47T79.
KW   Acyltransferase {ECO:0000256|RuleBase:RU365045};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000434};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000434};
KW   Transferase {ECO:0000256|RuleBase:RU365045,
KW   ECO:0000313|EMBL:AAZ54338.1}.
FT   DOMAIN       30    177       N-acetyltransferase.
FT                                {ECO:0000259|PROSITE:PS51186}.
SQ   SEQUENCE   190 AA;  21152 MW;  94943F8DC975CA00 CRC64;
     MFGQQAPSED RHSSDTESNH SLKAGEAADV ALEPPTLDDG RQLWALARIS DLDVNSPYAY
     VLWCRDFAAT SLVARDSTGT IRGFVTGYVR PDAPDTYFLW QVAVDPAFRG RRLARRMLDR
     ISSCITERGI RYLEATVTPG NTASRALFAS FARARSAALS WTPLFDRGHF PAELPEQHEP
     EDLVRIGPLR
//

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