ID A0A172TXX6_9BACT Unreviewed; 472 AA.
AC A0A172TXX6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Amino acid decarboxylase {ECO:0000313|EMBL:ANE51890.1};
GN ORFNames=SY85_16715 {ECO:0000313|EMBL:ANE51890.1};
OS Flavisolibacter tropicus.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Flavisolibacter.
OX NCBI_TaxID=1492898 {ECO:0000313|EMBL:ANE51890.1, ECO:0000313|Proteomes:UP000077177};
RN [1] {ECO:0000313|Proteomes:UP000077177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LCS9 {ECO:0000313|Proteomes:UP000077177};
RA Kim M.K., Srinivasan S., Lee J.-J.;
RT "Flavisolibacter sp./LCS9/ whole genome sequencing.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ANE51890.1, ECO:0000313|Proteomes:UP000077177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LCS9 {ECO:0000313|EMBL:ANE51890.1,
RC ECO:0000313|Proteomes:UP000077177};
RX PubMed=27259556; DOI=10.1099/ijsem.0.001207;
RA Lee J.J., Kang M.S., Kim G.S., Lee C.S., Lim S., Lee J., Roh S.H., Kang H.,
RA Ha J.M., Bae S., Jung H.Y., Kim M.K.;
RT "Flavisolibacter tropicus sp. nov., isolated from tropical soil.";
RL Int. J. Syst. Evol. Microbiol. 66:3413-3419(2016).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP011390; ANE51890.1; -; Genomic_DNA.
DR RefSeq; WP_066406028.1; NZ_CP011390.1.
DR AlphaFoldDB; A0A172TXX6; -.
DR STRING; 1492898.SY85_16715; -.
DR KEGG; fla:SY85_16715; -.
DR PATRIC; fig|1492898.3.peg.3638; -.
DR OrthoDB; 9803665at2; -.
DR Proteomes; UP000077177; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000077177}.
FT MOD_RES 296
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 472 AA; 52085 MW; 851AFD451C913178 CRC64;
MNTQLQQDLD NLSEILNAAK EQSLAYLGDI HKRPTTINQV PSLNNPTLPS QGQGALHTIQ
EFENRFQSLM VASSGPRYWG FVTGGSTPAA IMGDWLTSVY DQNTQSTKGQ GDLSALIESE
TINLLLQLFQ LPATYLGGFV TGATMSNFTC LAVARQWAGK QKGIDIAKEG VTSGIKILSA
TPHSSAIKSL AMLGLGSNHC LPVKVVNGNR EAMDIQDLEE KLRAYNGEPC IVISSGGTVN
TVDFDDMQAI AALKKKYNFW WHVDAAFGAF AACSPDYQHL LSGWDAADSI TVDGHKWLNV
PYDSAIFLIQ EKHRHLQVET FQNSNAPYLG DPLENFTYLN FLPENSRRLR ALPAWFTLMA
YGKDGYQQIV ENSINLSRQL GKRIESSELF ELLAPVRLNT VCFTLGRSKD QPETVKAFLT
ELNSRGKVFM TPTVYKGVSG IRAALVNWRT TSEDINLVWA EMEAAYLSVK AN
//
