ID A0A1I6ILV8_9MICO Unreviewed; 482 AA.
AC A0A1I6ILV8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=L-2,4-diaminobutyrate decarboxylase {ECO:0000313|EMBL:SFR67722.1};
GN ORFNames=SAMN05428970_0261 {ECO:0000313|EMBL:SFR67722.1};
OS Agromyces sp. CF514.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Agromyces.
OX NCBI_TaxID=1881031 {ECO:0000313|EMBL:SFR67722.1, ECO:0000313|Proteomes:UP000199174};
RN [1] {ECO:0000313|EMBL:SFR67722.1, ECO:0000313|Proteomes:UP000199174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF514 {ECO:0000313|EMBL:SFR67722.1,
RC ECO:0000313|Proteomes:UP000199174};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOZD01000001; SFR67722.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6ILV8; -.
DR STRING; 1881031.SAMN05428970_0261; -.
DR OrthoDB; 3335676at2; -.
DR Proteomes; UP000199174; 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; 3.90.1150.10; 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}.
FT MOD_RES 298
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 482 AA; 51708 MW; A03BEAB50D9454E4 CRC64;
MRDLLMSSTV TEYTDLLGRA TGLVADRVAS VTQPFSGASR AELQHLVDAV DLESAGVGTA
EALREVDELF LEHAIWFHDP AYTAHLNCPV ALPAVAAEAI LAAVNPSVDT YDQSAVGTLM
ERRLVTWTAQ RIGFEHGDGV FTSGGTQSNL HALLLAREWT LGRHERSRAE LLPRLNILAT
ASSHFSVEKS ALLLGLGDDA VVSVPDDGEG RMDAAALAAS LAAIRAAGRI PMAVVATAGT
TDRGVIDPVA AIAEHCDAHE VWLHVDAAYG CGLLVSKQHR GLISGIERAR SVTVDFHKSF
FQPVSSSTIV VREPGDLAAA AWHADYLNPL ENDEPNQVDK SLQTTRRFDA LKLWMTLRAL
GADRIGEMFD EVIELARVVG DGIAADPELE LVGRSQLSTV LFRVRPEGAD EATQDALVAQ
VRRVLFESGR ALVAKTVIDG RPCLKLTLLN PEASVADIRH VLDLVKDAAA TLVDLRDVEV
VA
//