ID A0A066Z1J4_9ACTN Unreviewed; 479 AA.
AC A0A066Z1J4;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Amino acid decarboxylase {ECO:0000313|EMBL:KDN87382.1};
GN ORFNames=KCH_08730 {ECO:0000313|EMBL:KDN87382.1};
OS Kitasatospora cheerisanensis KCTC 2395.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Kitasatospora.
OX NCBI_TaxID=1348663 {ECO:0000313|EMBL:KDN87382.1, ECO:0000313|Proteomes:UP000027178};
RN [1] {ECO:0000313|EMBL:KDN87382.1, ECO:0000313|Proteomes:UP000027178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 2395 {ECO:0000313|EMBL:KDN87382.1,
RC ECO:0000313|Proteomes:UP000027178};
RA Nam D.H.;
RT "Draft Genome Sequence of Kitasatospora cheerisanensis KCTC 2395.";
RL Submitted (MAY-2014) 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:KDN87382.1}.
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DR EMBL; JNBY01000037; KDN87382.1; -; Genomic_DNA.
DR RefSeq; WP_051652713.1; NZ_KK853997.1.
DR AlphaFoldDB; A0A066Z1J4; -.
DR PATRIC; fig|1348663.4.peg.829; -.
DR eggNOG; COG0076; Bacteria.
DR HOGENOM; CLU_011856_0_4_11; -.
DR OrthoDB; 3335676at2; -.
DR Proteomes; UP000027178; 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:UP000027178}.
FT MOD_RES 295
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 479 AA; 51337 MW; 4BB4FCCDF85043A2 CRC64;
MNDDFRTAAR ATAQLVADYL DELPSRPVWQ PMDPAERSAL LELTLPEDGV GFEELLKTVE
RTIMPHPMGN GNPRFFGWVN SAPQPAGVLA TLAASAMNPS SAGGDHADVH LERAVVRWIA
ELVGFPHPAG GGLLTSGTSM ATIVCLAAAR DRAARNAGRD VRQDGLAGMP PLVGYVTGEA
HSCVRKAAEL LGLGSKHLRV VEADAEGHLR LDSLEAAIAE DRAAGRLPFL VVASAGTVGT
GAVDPFEPIA DLAAREGLWF HVDGAYGAFG VLDPQIAHRY AGLERADSLA LDPHKWLGVP
VDCGCALVRD AQELRGTFSL VPSYLRDEDA GGLGWFSEYG TEQTRPFRSL KVWASIAHRG
RSGVARDIAH CTGQARRLGV WVEQDPELEL LAPVETSIVA FRYRPAGLDE EAVQRLNSLL
PVAVQQRGRV FVTGAVYRGQ EMLRACLLNA ATTDADLRLL LDEVKSAGAE LLDRGRTSM
//
