ID   A0A1H1ZFP0_9ACTN        Unreviewed;       425 AA.
AC   A0A1H1ZFP0;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=L-histidine carboxy-lyase (Histamine-forming) {ECO:0000313|EMBL:SDT32534.1};
GN   ORFNames=SAMN04489716_3300 {ECO:0000313|EMBL:SDT32534.1};
OS   Actinoplanes derwentensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=113562 {ECO:0000313|EMBL:SDT32534.1, ECO:0000313|Proteomes:UP000198688};
RN   [1] {ECO:0000313|EMBL:SDT32534.1, ECO:0000313|Proteomes:UP000198688}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43941 {ECO:0000313|EMBL:SDT32534.1,
RC   ECO:0000313|Proteomes:UP000198688};
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; LT629758; SDT32534.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1ZFP0; -.
DR   STRING; 113562.SAMN04489716_3300; -.
DR   Proteomes; UP000198688; Chromosome i.
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   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; PTHR46101; -; 1.
DR   PANTHER; PTHR46101:SF2; SERINE DECARBOXYLASE; 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:UP000198688}.
FT   MOD_RES         252
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   425 AA;  46161 MW;  C4DFAEF4D3613366 CRC64;
     MTPSVIPPED WSEAIRLGRT PALIDIEAVI DTLVIRANRA QRRTIGFPAA TDIDWSRTRG
     LFSRLFNNVG DPSTAPGGEA HTNSLEVEVV QWFADVVGLP QNDRWGYVTS GGTESNIAAL
     RVARDRYPDA VLYLTHASHY SIPKTASLLG LHPSDVVLVE DGRYGEMDYE HFEYLVSQRR
     DRPAIVVATA GTTLWEAVDQ TDQIEAILHG YGVDRRHVHV DAALSGIPLA LDGMLGLGAG
     SPVDSVSISG HKFLGTPIPC GVVVMRDSVR VSKGEHVNYV ATVDSTISGS RCGQASALLW
     AAIAMYGRNG HHSRAEHARQ IAAYAVERIS SLGWPVYRHP AAFTVVMQTP PPVLVSDFGW
     VLSVDGDLCH IICMPGIERD VIDDFVSDLG KVIGRPVLVP HRRRNTRSES AWRTAAAGDD
     QLVSG
//