ID S4M502_9ACTN Unreviewed; 487 AA.
AC S4M502;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Putative Tyrosine decarboxylase 1 {ECO:0000313|EMBL:EPJ34268.1};
GN ORFNames=STAFG_8677 {ECO:0000313|EMBL:EPJ34268.1};
OS Streptomyces afghaniensis 772.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1283301 {ECO:0000313|EMBL:EPJ34268.1, ECO:0000313|Proteomes:UP000015001};
RN [1] {ECO:0000313|EMBL:EPJ34268.1, ECO:0000313|Proteomes:UP000015001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=772 {ECO:0000313|EMBL:EPJ34268.1,
RC ECO:0000313|Proteomes:UP000015001};
RA Gruening B.A., Praeg A., Erxleben A., Guenther S., Fiedler H.-P.,
RA Goodfellow M., Mueller M.;
RT "Draft Genome Sequence of Streptomyces afghaniensis, Which Produces
RT Compounds of the Julimycin B-Complex.";
RL Submitted (FEB-2013) 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:EPJ34268.1}.
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DR EMBL; AOPY01001706; EPJ34268.1; -; Genomic_DNA.
DR RefSeq; WP_020277494.1; NZ_KE354488.1.
DR AlphaFoldDB; S4M502; -.
DR PATRIC; fig|1283301.3.peg.8610; -.
DR HOGENOM; CLU_011856_0_4_11; -.
DR OrthoDB; 3335676at2; -.
DR Proteomes; UP000015001; 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 GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
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:UP000015001}.
FT MOD_RES 305
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 487 AA; 53066 MW; E2A5930984D81DD3 CRC64;
MSPHEETTPL DPPDWEEFKA LGRRIVDDMA DYLAGIRDRP VWQPVPPDVQ ARLGTALPRT
PTPVQDVYEE FRTTVMPYPR GNIHPRFWGW ANGSGVPVAA YADLLASVVN CTLGSGENAA
MMVEHQVLEW LKEAMRWPAD GSGILTSGAS MGQIIALAAA RRAKSGTADI RGLGALADGR
QFTVYGSTQT HHSVEKAVEL LGIGGQYFRQ TPVDAAFRID TGALRRAIRA DRDAGLHPLC
LVGNAGTVNT GAVDPLDELL AIAREEDLWF HVDGAFGAFA QLLPTHRTLL AGMSEADSLV
FDLHKWLYMP FDVSCVLVRR ADALESTFSS SADYISSTDQ GPAAYSLAFS DRGVEQSRRF
RALKVWFALK THGIESFAAS IAGNIGQIAH LTKLADSSDR LEVVSRSDLN IVCFRYVRPG
ATADELNRLN QAVLTRLQVG GLAMPSHTVI DGKFVIRVAN NNHRSELSDF DFLVEQVVAI
GDELIAT
//
