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PAPC_STRPR
ID   PAPC_STRPR              Reviewed;         296 AA.
AC   P72540;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=4-amino-4-deoxyprephenate dehydrogenase;
DE            EC=1.3.1.121 {ECO:0000305|PubMed:9044253};
GN   Name=papC {ECO:0000303|PubMed:9044253};
GN   ORFNames=SPRI_0305 {ECO:0000312|EMBL:ALC18611.1},
GN   SPRI_7048 {ECO:0000312|EMBL:ALC25354.1};
OS   Streptomyces pristinaespiralis.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=38300;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC   STRAIN=SP92;
RX   PubMed=9044253; DOI=10.1046/j.1365-2958.1997.2031574.x;
RA   Blanc V., Gil P., Bamas-Jacques N., Lorenzon S., Zagorec M.,
RA   Schleuniger J., Bisch D., Blanche F., Debussche L., Crouzet J., Thibaut D.;
RT   "Identification and analysis of genes from Streptomyces pristinaespiralis
RT   encoding enzymes involved in the biosynthesis of the 4-dimethylamino-L-
RT   phenylalanine precursor of pristinamycin I.";
RL   Mol. Microbiol. 23:191-202(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Pr11;
RX   PubMed=21342465; DOI=10.1111/j.1751-7915.2010.00213.x;
RA   Mast Y., Weber T., Golz M., Ort-Winklbauer R., Gondran A., Wohlleben W.,
RA   Schinko E.;
RT   "Characterization of the 'pristinamycin supercluster' of Streptomyces
RT   pristinaespiralis.";
RL   Microb. Biotechnol. 4:192-206(2011).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HCCB 10218;
RA   Tian J., Yang J., Li L., Ruan L., Wei W., Zheng G., Wei Z., Yang S., Ge M.,
RA   Jiang W., Lu Y.;
RT   "Genome sequence of the pristinamycin over-producing bacterium Streptomyces
RT   pristinaespiralis HCCB10218.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in pristinamycin I biosynthesis (PubMed:9044253).
CC       Probably catalyzes the formation of 3-(4-aminophenyl)pyruvate from 4-
CC       amino-4-deoxyprephenate (Probable). {ECO:0000269|PubMed:9044253,
CC       ECO:0000305|PubMed:9044253}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-amino-4-deoxyprephenate + NAD(+) = 3-(4-aminophenyl)pyruvate
CC         + CO2 + H(+) + NADH; Xref=Rhea:RHEA:59380, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:143070, ChEBI:CHEBI:143071; EC=1.3.1.121;
CC         Evidence={ECO:0000305|PubMed:9044253};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59381;
CC         Evidence={ECO:0000305|PubMed:9044253};
CC   -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:9044253}.
CC   -!- SIMILARITY: Belongs to the prephenate/arogenate dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; U60417; AAC44867.1; -; Genomic_DNA.
DR   EMBL; FR682001; CBW45754.1; -; Genomic_DNA.
DR   EMBL; CP011340; ALC18611.1; -; Genomic_DNA.
DR   EMBL; CP011340; ALC25354.1; -; Genomic_DNA.
DR   RefSeq; WP_053556639.1; NZ_CP011340.1.
DR   SMR; P72540; -.
DR   STRING; 38300.SPRI_0305; -.
DR   EnsemblBacteria; ALC18611; ALC18611; SPRI_0305.
DR   EnsemblBacteria; ALC25354; ALC25354; SPRI_7048.
DR   KEGG; spri:SPRI_0305; -.
DR   KEGG; spri:SPRI_7048; -.
DR   PATRIC; fig|38300.4.peg.320; -.
DR   OrthoDB; 533829at2; -.
DR   Proteomes; UP000060513; Chromosome.
DR   GO; GO:0008977; F:prephenate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0004665; F:prephenate dehydrogenase (NADP+) activity; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006571; P:tyrosine biosynthetic process; IEA:InterPro.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR003099; Prephen_DH.
DR   Pfam; PF02153; PDH; 1.
DR   SUPFAM; SSF48179; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS51176; PDH_ADH; 1.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis; Oxidoreductase.
FT   CHAIN           1..296
FT                   /note="4-amino-4-deoxyprephenate dehydrogenase"
FT                   /id="PRO_0000453961"
FT   DOMAIN          9..288
FT                   /note="Prephenate/arogenate dehydrogenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00522"
SQ   SEQUENCE   296 AA;  30184 MW;  A12B75F1B03931A2 CRC64;
     MRGGSVFGRC VVVGGAGAVG RMFSHWLVRS GVAVTWLDVA GAGAADGVRV VAGDVRRPGP
     EAVAALAAAD VVVLAVPEPV AWEAVEVLAG VMRPGAVLAD TLSVKSRIAG RLREAAPGLQ
     AVGLNPMFAP SLGLQGRPVA AVVVTDGPGV RALVELVAGW GARVVEMPAR RHDELTAAQQ
     AATHAAVLAF GLGLGELSVD VGALRDSAPP PHLAMLALLA RIAGGTPEVY FDIQAANPGA
     PAARQALGRG LVRLGQAVER GDEETFAALF AELRGVLGEH GAELERLCAR MFTALH
 
 
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