ID   A6VVT5_MARMS            Unreviewed;       383 AA.
AC   A6VVT5;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   SubName: Full=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:ABR70564.1};
GN   OrderedLocusNames=Mmwyl1_1637 {ECO:0000313|EMBL:ABR70564.1};
OS   Marinomonas sp. (strain MWYL1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinomonas.
OX   NCBI_TaxID=400668 {ECO:0000313|EMBL:ABR70564.1};
RN   [1] {ECO:0000313|EMBL:ABR70564.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MWYL1 {ECO:0000313|EMBL:ABR70564.1};
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., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Johnston A.W.B., Todd J.D., Rogers R., Wexler M., Bond P.L., Li Y.,
RA   Richardson P.;
RT   "Complete sequence of Marinomonas sp. MWYL1.";
RL   Submitted (JUN-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; CP000749; ABR70564.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6VVT5; -.
DR   STRING; 400668.Mmwyl1_1637; -.
DR   KEGG; mmw:Mmwyl1_1637; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_028929_0_2_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:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR021115; Pyridoxal-P_BS.
DR   PANTHER; PTHR46101; -; 1.
DR   PANTHER; PTHR46101:SF2; SERINE DECARBOXYLASE; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 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         233
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   383 AA;  43599 MW;  8DB3231D02F367E1 CRC64;
     MNLSIANKER LDSFWSYCLQ HQYFNIGYPE SADFDYSSLY RFFNFSLNNC GDWRELSNYA
     LNSFEFEEDV MQYFAELFKI SFQESWGYVT NGGTEGNMFG CYLARELFPN STLYYSKETH
     YSVAKIAKLL RMKSCLVDTL DNGEINTDDL IQKILFNKDK QPIIFANIGT TMSGAVDNIA
     NIQLQLKQIH IDRHNYYLHA DAALSGMILP FVNNPQPFTF ADGIDSISVS GHKMIGSPIP
     CGVVVAKCKN VDRISVDVDY ISARDQTISG SRNAHSVLMM WSAIHSHSPL EWRQRIEHCL
     NMAQYAVNKF QAAGIRAWRN PNSITVVFPS PSEKVSRHYH LAVSGASAHL ITMPHHKTTQ
     KIDELIQAII LDQRELLEHS AYS
//