ID A0A084A645_9GAMM Unreviewed; 471 AA.
AC A0A084A645;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=L-2,4-diaminobutyrate decarboxylase {ECO:0000313|EMBL:KEY60774.1};
DE EC=4.1.1.86 {ECO:0000313|EMBL:KEY60774.1};
GN Name=ddc {ECO:0000313|EMBL:KEY60774.1};
GN ORFNames=SRDD_02720 {ECO:0000313|EMBL:KEY60774.1};
OS Serratia sp. DD3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=1410619 {ECO:0000313|EMBL:KEY60774.1, ECO:0000313|Proteomes:UP000017810};
RN [1] {ECO:0000313|EMBL:KEY60774.1, ECO:0000313|Proteomes:UP000017810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD3 {ECO:0000313|EMBL:KEY60774.1,
RC ECO:0000313|Proteomes:UP000017810};
RX PubMed=25212623;
RA Poehlein A., Freese H.M., Daniel R., Simeonova D.D.;
RT "Draft Genome Sequence of Serratia sp. Strain DD3, Isolated from the Guts
RT of Daphnia magna.";
RL Genome Announc. 2:e00903-14(2014).
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}.
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:KEY60774.1}.
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DR EMBL; AYKS02000014; KEY60774.1; -; Genomic_DNA.
DR RefSeq; WP_023491664.1; NZ_AYKS02000014.1.
DR AlphaFoldDB; A0A084A645; -.
DR STRING; 1410619.SRDD_02720; -.
DR eggNOG; COG0076; Bacteria.
DR OrthoDB; 9803665at2; -.
DR Proteomes; UP000017810; Unassembled WGS sequence.
DR GO; GO:0033983; F:diaminobutyrate decarboxylase activity; IEA:UniProtKB-EC.
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 InterPro; IPR021115; Pyridoxal-P_BS.
DR PANTHER; PTHR11999:SF70; AROMATIC-L-AMINO-ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR PRINTS; PR00800; YHDCRBOXLASE.
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:UP000017810}.
FT MOD_RES 298
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 471 AA; 51392 MW; 44AF3AFB64468091 CRC64;
MHWRLQQDLD NYPEILNCAT QLAQNFLSGL DRRSVCPPLM DQQIKPDDQQ LSPEGKGAVA
ALEYFWHHYA AGLSASAGPR YFGFVTGGVT PAALAADWLV STVDQNSLLS HDTVAAAIEL
ATIEQLKILL GLPAQFSGSF VSGATMANFV GIAIGRQWLG QQQGVDIAQQ GVTALGPIQV
LSANAHSSSV KALSMLGLGR DSLKVIARQK DSEVIDTVAL EQHLAVTQGI PTIVLASAGT
VNTAVFDDLP RLLALRERYP FWLHVDGAFG GVAACSPIHA HLLAGWEQAD SITVDAHKWL
NVPYDCAIQF TRHLALQLQV FQNHSAYLEA PTLRPDNYLH LTPENSRRFR ALPLWMALKA
YGRHGVQEIV ERNVTLARQL GHQLAASEGF CLLAPVNLNV VCFALKNISG DAAMTRDRFL
SYLDQQGIVR CTPTQYNGQP AIRAALVNWM TQEHDIQLAL ESLLACRAQI D
//
