ID L8JQS2_9BACT Unreviewed; 469 AA.
AC L8JQS2;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Aromatic-L-amino-acid decarboxylase {ECO:0000313|EMBL:ELR70573.1};
GN ORFNames=C900_03554 {ECO:0000313|EMBL:ELR70573.1};
OS Fulvivirga imtechensis AK7.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Fulvivirgaceae;
OC Fulvivirga.
OX NCBI_TaxID=1237149 {ECO:0000313|EMBL:ELR70573.1, ECO:0000313|Proteomes:UP000011135};
RN [1] {ECO:0000313|EMBL:ELR70573.1, ECO:0000313|Proteomes:UP000011135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK7 {ECO:0000313|EMBL:ELR70573.1,
RC ECO:0000313|Proteomes:UP000011135};
RA Nupur N., Khatri I., Kumar R., Subramanian S., Pinnaka A.;
RT "Genome assembly of Fulvivirga imtechensis AK7.";
RL Submitted (DEC-2012) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ELR70573.1}.
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DR EMBL; AMZN01000051; ELR70573.1; -; Genomic_DNA.
DR RefSeq; WP_009580930.1; NZ_AMZN01000051.1.
DR AlphaFoldDB; L8JQS2; -.
DR STRING; 1237149.C900_03554; -.
DR PATRIC; fig|1237149.3.peg.3315; -.
DR eggNOG; COG0076; Bacteria.
DR OrthoDB; 9803665at2; -.
DR Proteomes; UP000011135; Unassembled WGS sequence.
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 CDD; cd06450; DOPA_deC_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 1.20.1340.10; dopa decarboxylase, N-terminal domain; 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 InterPro; IPR021115; Pyridoxal-P_BS.
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.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000011135}.
FT MOD_RES 294
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 469 AA; 53241 MW; 21EF7066A240F7D6 CRC64;
MNIEEFKKYG HEIVEWIASY YENIRDYPVR SQVSPGEIFN KLDGAAPEEG EQMSRILKDF
EDIIMPGITH WQSPAFHAYF PSNTSFPSLL GEMLTSALGA QCMIWDTSPA AAELEEKVMI
WLRDMIGLPE SFSGVTQDTA STATLCALIT AREKKSNFGV NSNGFFDQKP MRIYCSAETH
SSVEKAVKIM GAGNNNLVKV GVDDNQAVDI RLLRQAIRKD IEAGFQPLAV VAAIGTTGTV
AIDPLKEIAA VCREFDLWLH VDAAYAGTAL ILEEYRWMIE GIEDVDSFVF NPHKWMFVNF
DCSAYFVKDE KALSNTFSIL PEYLKTNTTG KVKDYRDWSI QLGRSFRALK LWFVIRSYGV
NQMKKIIREH INMAKSLAEM IREHSGFEVL TVSLNLICFR LRPYQAESLE EINQRNKNLM
DKLNASGKIY LTHTKIGDKL VLRMVTGQTY LTEADVRRSW EVIKEAVER
//
