ID A0A0U3H8C9_9MICC Unreviewed; 494 AA.
AC A0A0U3H8C9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:ALU39157.1};
GN ORFNames=AS188_04620 {ECO:0000313|EMBL:ALU39157.1}, KFL01_02250
GN {ECO:0000313|EMBL:GEO90919.1};
OS Kocuria flava.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Kocuria.
OX NCBI_TaxID=446860 {ECO:0000313|EMBL:ALU39157.1, ECO:0000313|Proteomes:UP000057181};
RN [1] {ECO:0000313|EMBL:ALU39157.1, ECO:0000313|Proteomes:UP000057181}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HO-9041 {ECO:0000313|EMBL:ALU39157.1,
RC ECO:0000313|Proteomes:UP000057181};
RA Zhou M., Dai J.;
RT "Complete Genome Sequence of Kocuria flava strain HO-9041.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GEO90919.1, ECO:0000313|Proteomes:UP000321155}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 107626 {ECO:0000313|EMBL:GEO90919.1,
RC ECO:0000313|Proteomes:UP000321155};
RA Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT "Whole genome shotgun sequence of Kocuria flava NBRC 107626.";
RL Submitted (JUL-2019) 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; CP013254; ALU39157.1; -; Genomic_DNA.
DR EMBL; BJZR01000003; GEO90919.1; -; Genomic_DNA.
DR RefSeq; WP_058857869.1; NZ_CP013254.1.
DR AlphaFoldDB; A0A0U3H8C9; -.
DR STRING; 446860.AS188_04620; -.
DR KEGG; kfv:AS188_04620; -.
DR OrthoDB; 3335676at2; -.
DR Proteomes; UP000057181; Chromosome.
DR Proteomes; UP000321155; 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 Gene3D; 3.90.1150.170; -; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 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; PTHR45677:SF8; CYSTEINE SULFINIC ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 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:UP000057181}.
FT MOD_RES 303
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 494 AA; 52746 MW; 25C245B0AEAB2E9E CRC64;
MHDFLLSRST PGQYARALHS TVDTVAVHLA GTRAPRSDAG PAELEQLVAA VDLDRPLGDL
EAVLEETRAL YLDHAVHFHD PGYMAHLNCP VAIPAVAAEA FTAATNTAVE SWDQSTVATL
VEQRLVDWTA DRIGFPAADG PDGVFTSGGT QSNLQALFTA REERLSRPHP RARQDRLGRL
RVLAGEHAHF SVARAAHLLG LPRDAVVALP ARRDGCLDPV ALERALHGAA AAGDEVMAVV
ATAGSTDLGL IDPLPAVADA CRAHGAWLHV DAAYGGGLLV SPSHRGLLDG IERADSVTVD
FHKSWFQPVA ASALLLREGR HLGLSTWSAE YLNPRHAVRP NLVDKSLQTT RRFDALKLWM
TLRTVGAEAL GRSLDRAVDL AREAAAAVAA APDMELLGEP ALSTVLFRHR PPGTGEAEAD
RLVETVRTAL FDTGRAVVAS TVVGGRRWLK LTLLNPRTDL ADVEHVLGLV REAAREAARE
AAREQAPLST AGAR
//
