ID   B6B4G5_9RHOB            Unreviewed;       470 AA.
AC   B6B4G5;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=Tyrosine decarboxylase 1 {ECO:0000313|EMBL:EDZ48207.1};
DE            EC=4.1.1.25 {ECO:0000313|EMBL:EDZ48207.1};
GN   ORFNames=RBY4I_3427 {ECO:0000313|EMBL:EDZ48207.1};
OS   Rhodobacterales bacterium Y4I.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales.
OX   NCBI_TaxID=439496 {ECO:0000313|EMBL:EDZ48207.1, ECO:0000313|Proteomes:UP000005133};
RN   [1] {ECO:0000313|EMBL:EDZ48207.1, ECO:0000313|Proteomes:UP000005133}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4I {ECO:0000313|EMBL:EDZ48207.1,
RC   ECO:0000313|Proteomes:UP000005133};
RA   Moran M.A., Buchan A., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA   Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUL-2008) 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; DS995281; EDZ48207.1; -; Genomic_DNA.
DR   AlphaFoldDB; B6B4G5; -.
DR   STRING; 439496.RBY4I_3427; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_011856_3_1_5; -.
DR   OrthoDB; 9803665at2; -.
DR   Proteomes; UP000005133; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0004837; F:tyrosine decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
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   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:UP000005133}.
FT   MOD_RES         295
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   470 AA;  52797 MW;  61DA2D7E0427D170 CRC64;
     MNWDEFSEWG RRVADWTQDY HLTVGDRPVR ARTKPGEVLN ALPQTPPEAG EGMEAIFRDF
     EDIVMPGITH WQHPRFFAYF TSNAAAPSVL AEFLASAIAP QCMLWQTSPA ATEMETRMMD
     WLRQALDLPE QFQGVIQDSA SSATLAAVLT MREKALNWQG NQQGLFAQKP LRIYCSSEVH
     TSIDRAIWVA GIGQQNLIRI PIKGGWRGMD PGALEAAIQA DLAAGHQPAG VILCVGGTGV
     GATDPVDKVL DVAEKYGLYT HVDAAWAGSA MICPEYRHYW PGVERADSIV FNPHKWLGVQ
     FDCSAHFLKN PDDLVKTLAI SPEYLKTHGH DGIINYSEWS VPLGRRFRAL KIWFLIRTYG
     LEGLRQRLRN HITWSNQLHD KLKSEPDFEI TTPPMWSLWS FRYAPEGAAD LDDLNLRLVN
     AINDDGRIYL TQTRLDGQLV IRFQAGQFET TEADVMTAFD VITEIARSLT
//