ID   PANP_ALIF1              Reviewed;         547 AA.
AC   Q5E6F9;
DT   05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Aspartate 1-decarboxylase {ECO:0000303|PubMed:28446608};
DE            EC=4.1.1.11 {ECO:0000269|PubMed:28446608};
GN   Name=panP {ECO:0000303|PubMed:28446608};
GN   OrderedLocusNames=VF_0892 {ECO:0000312|EMBL:AAW85387.1};
OS   Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=312309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700601 / ES114;
RX   PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA   Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA   Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA   Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT   "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT   pathogenic congeners.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 700601 / ES114;
RX   PubMed=28446608; DOI=10.1074/jbc.m116.763193;
RA   Pan S., Nikolakakis K., Adamczyk P.A., Pan M., Ruby E.G., Reed J.L.;
RT   "Model-enabled gene search (MEGS) allows fast and direct discovery of
RT   enzymatic and transport gene functions in the marine bacterium Vibrio
RT   fischeri.";
RL   J. Biol. Chem. 292:10250-10261(2017).
CC   -!- FUNCTION: Catalyzes the pyridoxal-dependent decarboxylation of
CC       aspartate to produce beta-alanine. Has weak activity with glutamate.
CC       {ECO:0000269|PubMed:28446608}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-aspartate = beta-alanine + CO2; Xref=Rhea:RHEA:19497,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:29991,
CC         ChEBI:CHEBI:57966; EC=4.1.1.11;
CC         Evidence={ECO:0000269|PubMed:28446608};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000269|PubMed:28446608};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.44 mM for aspartate (at 28 degrees Celsius)
CC         {ECO:0000269|PubMed:28446608};
CC         KM=1.70 mM for aspartate (at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:28446608};
CC         Note=kcat is 0.075 sec(-1) at 28 degrees Celsius. kcat is 0.008 sec(-
CC         1) at 37 degrees Celsius. {ECO:0000269|PubMed:28446608};
CC   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-
CC       alanine from L-aspartate: step 1/1. {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Deletion mutant cannot grow in minimal medium.
CC       {ECO:0000269|PubMed:28446608}.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000020; AAW85387.1; -; Genomic_DNA.
DR   RefSeq; WP_011261555.1; NC_006840.2.
DR   RefSeq; YP_204275.1; NC_006840.2.
DR   AlphaFoldDB; Q5E6F9; -.
DR   SMR; Q5E6F9; -.
DR   STRING; 312309.VF_0892; -.
DR   EnsemblBacteria; AAW85387; AAW85387; VF_0892.
DR   KEGG; vfi:VF_0892; -.
DR   PATRIC; fig|312309.11.peg.888; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_011856_0_4_6; -.
DR   OMA; RHATYHA; -.
DR   OrthoDB; 1478871at2; -.
DR   UniPathway; UPA00028; UER00002.
DR   Proteomes; UP000000537; Chromosome I.
DR   GO; GO:0004068; F:aspartate 1-decarboxylase activity; IDA:UniProtKB.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR022517; Asp_decarboxylase_pyridox.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR03799; NOD_PanD_pyr; 1.
PE   1: Evidence at protein level;
KW   Decarboxylase; Lyase; Pantothenate biosynthesis; Pyridoxal phosphate;
KW   Reference proteome.
FT   CHAIN           1..547
FT                   /note="Aspartate 1-decarboxylase"
FT                   /id="PRO_0000440874"
FT   MOD_RES         338
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y600"
SQ   SEQUENCE   547 AA;  60953 MW;  B089F65FD9D6844C CRC64;
     MVTDNKTADA SFESLLRIFT VPEAPDSTLG IIEKELSQNL NQFLREHIVA EEKPLTEIEK
     DFTDSSMPES PTYVSEHTEH LLDTLVSQSV HTSAPSFIGH MTSALPYFLM PLSKIMIALN
     QNLVKIETSK AFTPLERQVL GMLHRLIFGQ KDSFYQHWMH SADHSLGAFC SGGTIANITA
     LWVARNRLLK PEGDFEGIAK QGLFAALMHY KCNGLAIFVS ERGHYSLKKA ADVLGIGQDG
     VIAVKTDNNN RVCLDDLELK IAQAKAKNIK PLAIVGVAGT TETGSIDPLR ELANVAQREG
     CHFHVDAAWG GATLMSNTYR HLLDGIDLAD SVTIDAHKQL YVPMGAGMVI FKDPELMSSI
     QHHAEYILRK GSKDLGRHTL EGSRSGMAML LYSCFNVISR PGYELLINQS IEKAHYFADL
     IQQQDDFELI TEPELCLLTY RYVPSNVKAA LAIATDEQKI EIYEHLDNLT KYIQKTQRET
     GKSFVSRTRL TPEAYQHQPT IVFRVVLANP LTTKEILQNV LIEQREIASS SEISLPLLNQ
     IVGNILH