ID   A8GGB0_SERP5            Unreviewed;       471 AA.
AC   A8GGB0;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   SubName: Full=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:ABV42150.1};
GN   OrderedLocusNames=Spro_3049 {ECO:0000313|EMBL:ABV42150.1};
OS   Serratia proteamaculans (strain 568).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=399741 {ECO:0000313|EMBL:ABV42150.1};
RN   [1] {ECO:0000313|EMBL:ABV42150.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=568 {ECO:0000313|EMBL:ABV42150.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA   Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; CP000826; ABV42150.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8GGB0; -.
DR   STRING; 399741.Spro_3049; -.
DR   KEGG; spe:Spro_3049; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_011856_0_4_6; -.
DR   OrthoDB; 9803665at2; -.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR010977; Aromatic_deC.
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   PANTHER; PTHR11999:SF70; AROMATIC-L-AMINO-ACID DECARBOXYLASE; 1.
DR   PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   PRINTS; PR00800; YHDCRBOXLASE.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382}.
FT   MOD_RES         298
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   471 AA;  50998 MW;  BC6DDFEC8FC952D4 CRC64;
     MHPRLQQDLE QFPQILDRTR QLAEGFLTGL QQRPVCPPLA AQQLQPGDNL LADSGDGALA
     ALDDFWRRYA EGLSASAGPR YFGFVTGGST PAALAADWLV SAVDQNSQLS HDTVAAAIEL
     ATIVQLKDLL GLPEAFNGSF VSGATMANFV GMAIGRQWLG QQRGINVAEQ GLAALGAIQV
     LSANAHSSSE KALSMLGMGR DALKIIDSLP NSEAIDPTAL ERHLAASVGV PTMVLASAGT
     VNTVVFDDLQ QLLALRERYP FWLHVDAAFG GVAACSPHYA PRLAGWEQAD SITVDAHKWL
     NVPYDSAIQF SRHLALQMQV FQNHSAYLEA PTQRPDNYLH LTPENSRRFR ALPLWMALKA
     YGRSGMQDMV ERNVRLAQLL GAELTASAGF HLLAPVNLNV VCFALKNVAG DATAARDRFI
     ARLDRHGVVR CTPTRYNGQP GVRAALVNWM TEESDIHLAL ESIRHCLAET G
//