ID A0A0X8D5I0_9BACL Unreviewed; 551 AA.
AC A0A0X8D5I0;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=2,4-diaminobutyrate decarboxylase {ECO:0000313|EMBL:AMA74696.1};
GN ORFNames=ACH33_09885 {ECO:0000313|EMBL:AMA74696.1};
OS Aneurinibacillus sp. XH2.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC Aneurinibacillus group; Aneurinibacillus.
OX NCBI_TaxID=1450761 {ECO:0000313|EMBL:AMA74696.1, ECO:0000313|Proteomes:UP000065566};
RN [1] {ECO:0000313|Proteomes:UP000065566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xh2 {ECO:0000313|Proteomes:UP000065566};
RA Xi L.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AMA74696.1, ECO:0000313|Proteomes:UP000065566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xh2 {ECO:0000313|EMBL:AMA74696.1,
RC ECO:0000313|Proteomes:UP000065566};
RA Zhang Z., Qiao N., Zhang Y., Xiao Z., Jing L., Zhao J.-Y.;
RT "Draft genome of the novel themophilic polyhydroxyalkanoates producer
RT Aneurinibacillus sp. XH2 (CCTCC M 2013550) isolated from Gudao oilfield in
RT China.";
RL Submitted (JAN-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|RuleBase:RU000382}.
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DR EMBL; CP014140; AMA74696.1; -; Genomic_DNA.
DR RefSeq; WP_057900325.1; NZ_CP014140.1.
DR AlphaFoldDB; A0A0X8D5I0; -.
DR STRING; 1450761.ACH33_09885; -.
DR KEGG; anx:ACH33_09885; -.
DR Proteomes; UP000065566; 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:UP000065566}.
FT MOD_RES 335
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 551 AA; 61726 MW; 794D84251B4CB836 CRC64;
MKDIQALFPS EDGNKERRQV LLQFMQNIVE GLDRLKDPQR ATLGSMQERT GEFYKDIIDC
AQVPERGIAL DKVVEELLGL AKGHPYHTRN FVSNVLPMAS IPGILGSLLT TLLNGNNLWD
VYGPAGAEAE VKVIAMMSKL AGYDATKSWG YTTWGGQGAV FSGLRLAIAK QFPDAKEKGV
PGNLYCFASE NAHYSLFKSM EATGIGSNHL ITVKADPLTH AMNTDDLREK MERVIQQGGI
PIYIVATTGA TDSFGIDDIK AIKETADAIT NRYGLHPAHI HADSALGGFY CLFNDYDFAR
NPLQLEQPLC ENLLQIREKM QHLHLADSLC FDFQKLGQTP YLTSLFLVKN GKDIGLLDLH
EFETPYVGNR GYGSYHTSYT LECSRMASSI AIYAALLAFG VDGYRQILAN YVRVNMAFRD
RLLARFSNVA VTNENNPGPI TTFRFYPEQA EWHKERAGKL TGKQIKQNNE WNYPIFEELG
KHREHVFFGD TTRQCLVDAS DVSERVPVYA AKFFSISPYT TVETLDEIVE FLAKRVACVD
TMRNAREKTY V
//
