(data stored in SCRATCH zone)

SWISSPROT: A4F5T3_SACEN

ID   A4F5T3_SACEN            Unreviewed;       457 AA.
AC   A4F5T3;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   11-DEC-2019, entry version 63.
DE   SubName: Full=Glutamate/tyrosine decarboxylase-like PLP-dependent enzyme {ECO:0000313|EMBL:PFG93207.1};
DE   SubName: Full=Pyridoxal-dependent decarboxylase family protein, putative {ECO:0000313|EMBL:CAL99407.1};
DE            EC=4.1.1.- {ECO:0000313|EMBL:CAL99407.1};
GN   OrderedLocusNames=SACE_0054 {ECO:0000313|EMBL:CAL99407.1};
GN   ORFNames=A8924_0439 {ECO:0000313|EMBL:PFG93207.1};
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:CAL99407.1, ECO:0000313|Proteomes:UP000006728};
RN   [1] {ECO:0000313|EMBL:CAL99407.1, 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:CAL99407.1};
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA   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:PFG93207.1, ECO:0000313|Proteomes:UP000225825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40517 {ECO:0000313|EMBL:PFG93207.1,
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
CC         ECO:0000256|RuleBase:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; AM420293; CAL99407.1; -; Genomic_DNA.
DR   EMBL; PDBV01000001; PFG93207.1; -; Genomic_DNA.
DR   RefSeq; WP_009950420.1; NZ_PDBV01000001.1.
DR   STRING; 405948.SACE_0054; -.
DR   EnsemblBacteria; CAL99407; CAL99407; SACE_0054.
DR   KEGG; sen:SACE_0054; -.
DR   eggNOG; ENOG4107V4A; Bacteria.
DR   eggNOG; COG0076; LUCA.
DR   HOGENOM; HOG000253068; -.
DR   OMA; QPYGCGA; -.
DR   OrthoDB; 1478871at2; -.
DR   BioCyc; SERY405948:SACE_RS00260-MONOMER; -.
DR   Proteomes; UP000006728; Chromosome.
DR   Proteomes; UP000225825; Unassembled WGS sequence.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   3: Inferred from homology;
DR   PRODOM; A4F5T3.
DR   SWISS-2DPAGE; A4F5T3.
KW   Lyase {ECO:0000256|RuleBase:RU000382, ECO:0000313|EMBL:CAL99407.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006728}.
FT   MOD_RES         262
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   457 AA;  49365 MW;  093A1A27826844CF CRC64;
     MDLRRWLTTA VAEVERWQEE FGDFTTHPAA EVADQELGPA FAELAERLRD NYPFFHPRYA
     GQMIKPAHPA AVAGHLAAML VNPNNHALDG GPATARMERE VVARLAGVFG YGPDHLGHLT
     TSGTIANLEA LYVARETHPG RAVAHSADAH YTHSRMCRLL GVEAVPVPTD NAGRMDLDAL
     DSLLRTHDIG TVVLTAGTTG LGAIDPVHEA LALRERYGVR LHVDAAYGGF FTLIADDSPD
     GVASAPFQAL GACDSLVVDP HKHGLQPYGC GAVLFADPAA ERFYRHDSPY TYFTSAERHL
     GEVSLECSRA GAAAAALWLT FRLLPPTPDG LGRVLRPGRR AALRWADLLS ESPVLAPYQR
     PELDIVTYLP RAGRLSDIDA LSAAVLEGGM TAPAAESVFV ATYGVDRPAL AARGHEVEAD
     VAVGRILRSV LMKPEHDDWL DYLHTRIEEL VRTAAGR
//

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