ID   F9UIK6_9GAMM            Unreviewed;       492 AA.
AC   F9UIK6;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Aromatic-L-amino-acid decarboxylase {ECO:0000313|EMBL:EGV15960.1};
DE            EC=4.1.1.28 {ECO:0000313|EMBL:EGV15960.1};
GN   ORFNames=ThimaDRAFT_4759 {ECO:0000313|EMBL:EGV15960.1};
OS   Thiocapsa marina 5811.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Thiocapsa.
OX   NCBI_TaxID=768671 {ECO:0000313|EMBL:EGV15960.1, ECO:0000313|Proteomes:UP000005459};
RN   [1] {ECO:0000313|EMBL:EGV15960.1, ECO:0000313|Proteomes:UP000005459}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5811 {ECO:0000313|EMBL:EGV15960.1,
RC   ECO:0000313|Proteomes:UP000005459};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Cheng J.-F., Goodwin L., Pitluck S., Peters L.,
RA   Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J., Thiel V., Frigaard N.-U.,
RA   Bryant D., Woyke T.J.;
RT   "The draft genome of Thiocapsa marina 5811.";
RL   Submitted (JUN-2011) 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|RuleBase:RU000382}.
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DR   EMBL; AFWV01000028; EGV15960.1; -; Genomic_DNA.
DR   AlphaFoldDB; F9UIK6; -.
DR   STRING; 768671.ThimaDRAFT_4759; -.
DR   eggNOG; COG0076; Bacteria.
DR   OrthoDB; 9803665at2; -.
DR   Proteomes; UP000005459; Unassembled WGS sequence.
DR   GO; GO:0004058; F:aromatic-L-amino-acid decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.1150.170; -; 2.
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; 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:UP000005459}.
FT   MOD_RES         304
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   492 AA;  53222 MW;  15199BE97529D1C5 CRC64;
     MQKQNIKQSA LDPDDWDEYR VQAHRLLDVC VDHLQNARER PWRPVPDGIK QRLGLDDASS
     PSALSEVADE LLADILPFGT GNTHPRFFGW VHGTGLSIGV LADLVASTMN SNCGGRDHVA
     VYVERAVIDW CKRTFGFPDE ANGVLVTGTS QATVIALAVA RTRALGAGSR REGLRNGPAL
     AAYAREGVHI AIIKALELLG IGADALRRIP LDDAGAMDMA CLHEAVECDR EAGRVPFCLI
     GTAGSVDRGE FDDLQALAGF ARERELWFHI DGAFGAWVVL ADAPWNRLAA GIGQADSVAF
     DFHKWMYVQY DCGAVLIRDE ALHRQTFAGR PAYLADQVWG LGGGEPWFFD YGIDLSRGFR
     ALRVWAALRL HGSAAFGATI SRNCALALRM AECVSTAPEL ELAAPVRLNV CCFRAAPQGL
     AADAQDQLNV RIAQELQIAG SAVFSTTMVD GRIVLRAAIT NHRTDQQDVD ESVAAAAQLA
     QRLIALFLGE GE
//