ID Q65LZ2_BACLD Unreviewed; 542 AA.
AC Q65LZ2; Q62XC9;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE SubName: Full=Putative aminoacid decarboxylase {ECO:0000313|EMBL:AAU22579.1};
GN OrderedLocusNames=BL02887 {ECO:0000313|EMBL:AAU22579.1};
OS Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=279010 {ECO:0000313|EMBL:AAU22579.1, ECO:0000313|Proteomes:UP000000606};
RN [1] {ECO:0000313|EMBL:AAU22579.1, ECO:0000313|Proteomes:UP000000606}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB
RC 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46
RC {ECO:0000313|Proteomes:UP000000606};
RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA Rasmussen M.D., Andersen J.T., Jorgensen P.L., Larsen T.S., Sorokin A.,
RA Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT "Complete genome sequence of the industrial bacterium Bacillus
RT licheniformis and comparisons with closely related Bacillus species.";
RL Genome Biol. 5:R77.1-R77.12(2004).
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|RuleBase:RU000382}.
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DR EMBL; CP000002; AAU22579.1; -; Genomic_DNA.
DR AlphaFoldDB; Q65LZ2; -.
DR SMR; Q65LZ2; -.
DR STRING; 279010.BL02887; -.
DR KEGG; bli:BL02887; -.
DR eggNOG; COG0076; Bacteria.
DR HOGENOM; CLU_034727_0_0_9; -.
DR Proteomes; UP000000606; Chromosome.
DR GO; GO:0004058; F:aromatic-L-amino-acid decarboxylase activity; IEA:UniProt.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR PANTHER; PTHR45677:SF8; CYSTEINE SULFINIC ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR Pfam; PF00282; Pyridoxal_deC; 2.
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:UP000000606}.
FT MOD_RES 335
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 542 AA; 60385 MW; 05B410F758C83130 CRC64;
MVLDFQQMFP SEDGNHEARY QLLALLEAVL AGMDRLKDPG RLTLGRESEV SSDYYQSVIE
EAVLPEKGFG AEKSVEELLK LLDGHRFLNR HYVANATPLP NNASIAGNLL MVLLNGNNLW
DVDGTAAART EVQITAMLSD IVGYDRHKSG GFTTWGGQGA VFQSLRLAIA NAYPEANQQG
TPHHLYAFCS ELSHFSLYKS MEASGIGTDH LIKVKTNHDH SMDLADLREK MQAVIEKGGH
PIYVLATLGT TDAFGIDDLA GIKNVTEEIE AAYGLPPVYI HADTAMGGMY SFFNGYDFSG
NPLHIEDEVL ETLARYKQHF QHLHLADSLV FDFHKLGQTP YITSLFLVKN RKALQAVDLD
PDETPYVGNR GFGSYHTSYT LECSRMGSSI PIYASLLAFG IEGYQEILAN YIRVNLAFRK
KLLQAFPNAA VTNDVSPVTT FRFYPGNVRY HEEISGAITE EEVRNINKYN EKIAETLGRY
RSHTYFGSTK KQTYVYPADS RLPVPLYVQK FYSVSPYTTV DTTDQYIAFL KAHVETSDVA
AG
//
