ID A0A0J5P2T0_9PAST Unreviewed; 510 AA.
AC A0A0J5P2T0;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=2,4-diaminobutyrate decarboxylase {ECO:0000313|EMBL:KMK50793.1};
GN ORFNames=RO21_09785 {ECO:0000313|EMBL:KMK50793.1};
OS Muribacter muris.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Muribacter.
OX NCBI_TaxID=67855 {ECO:0000313|EMBL:KMK50793.1, ECO:0000313|Proteomes:UP000036270};
RN [1] {ECO:0000313|EMBL:KMK50793.1, ECO:0000313|Proteomes:UP000036270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ackerman80-443D {ECO:0000313|EMBL:KMK50793.1,
RC ECO:0000313|Proteomes:UP000036270};
RA Christensen H., Nicklas W., Bisgaard M.;
RT "Reclassification of Actinobacillus muris as Muribacter muris.";
RL Submitted (DEC-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|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:KMK50793.1}.
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DR EMBL; JWIZ01000068; KMK50793.1; -; Genomic_DNA.
DR RefSeq; WP_047977604.1; NZ_JWIZ01000068.1.
DR AlphaFoldDB; A0A0J5P2T0; -.
DR STRING; 67855.RO21_09785; -.
DR PATRIC; fig|67855.3.peg.2065; -.
DR Proteomes; UP000036270; 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:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR CDD; cd06450; DOPA_deC_like; 1.
DR Gene3D; 3.90.1150.170; -; 1.
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 InterPro; IPR021115; Pyridoxal-P_BS.
DR PANTHER; PTHR45677:SF8; CYSTEINE SULFINIC ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 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:UP000036270}.
FT MOD_RES 319
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 510 AA; 55702 MW; 772A7E717F574777 CRC64;
MTNLSQHKQA LFCNDAQSIA DYQTAMNEAV QAVSAWLKNE KMYTGGSIKQ LRSEIAFSPS
KAGLGVQKSL ARLVDLFLNK SLKVHHPHSL AHLHCPTMVA SQVAEVLINA TNQSMDSWDQ
SPAGSLMEVQ LIDWLRQKVG YGIGQAGVFT SGGTQSNLMG VLLARDACIA KHWQQADGSE
WSVQQAGLPP EALAKVKVLC SENAHFSVQK NMAMMGMGFQ SVITVPCRSN AQMDVAALAK
IIQEQTACGN IIACVVATAG TTDAGAIDPL AEISEICQQA GIWLHVDAAW GGALLLSNRY
RHFLNGLERA DSVTLDFHKH FFQTISCGAF LLKDEHNYRF IDYKADYLNS DYDEQHGVPN
LVAKSLQTTR RFDALKLWFT VEALGEDLYG SMIDHGVDLT RQVADYIQQT AGLELLVEPQ
FASVLFRVVP QGYPSEHLDA LNQNVADELF ARGEANIGVT KVGNVQSLKM TTLSPIATLD
NVKALLAQVQ SQADKIKEAI VKGEYIPPID
//
