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Database: UniProt
Entry: A0A078BAF4_STYLE
LinkDB: A0A078BAF4_STYLE
Original site: A0A078BAF4_STYLE 
ID   A0A078BAF4_STYLE        Unreviewed;       469 AA.
AC   A0A078BAF4;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Histidine decarboxylase {ECO:0000313|EMBL:CDW91535.1};
GN   Name=Contig1045.g1138 {ECO:0000313|EMBL:CDW91535.1};
GN   ORFNames=STYLEM_20691 {ECO:0000313|EMBL:CDW91535.1};
OS   Stylonychia lemnae (Ciliate).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Stylonychia.
OX   NCBI_TaxID=5949 {ECO:0000313|EMBL:CDW91535.1, ECO:0000313|Proteomes:UP000039865};
RN   [1] {ECO:0000313|EMBL:CDW91535.1, ECO:0000313|Proteomes:UP000039865}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=130c {ECO:0000313|EMBL:CDW91535.1,
RC   ECO:0000313|Proteomes:UP000039865};
RA   Swart Estienne;
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
CC         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; CCKQ01019517; CDW91535.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A078BAF4; -.
DR   EnsemblProtists; CDW91535; CDW91535; STYLEM_20691.
DR   InParanoid; A0A078BAF4; -.
DR   OrthoDB; 750143at2759; -.
DR   Proteomes; UP000039865; Unassembled WGS sequence.
DR   GO; GO:0016830; F:carbon-carbon 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   PANTHER; PTHR46101; -; 1.
DR   PANTHER; PTHR46101:SF18; HISTIDINE DECARBOXYLASE; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000039865}.
FT   COILED          134..161
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         305
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   469 AA;  53318 MW;  918C5C4780273E47 CRC64;
     MDFEEAERQR VWLMSGHIKK LGYQNACTTV LFNKYPTLDK IDTTFYPTNP DGTKNYKIVD
     SSVLGIIPGS LAETFNYCSG DPTDPDSKWQ NPHEQYVISQ MGKLLGIQDV TGYMSSGGTE
     GNLAAIWWCK TNLTTRSQSK IQELKDRIKQ HKNQQEVDYE EILNLKEKIS KLRRPYIVAT
     KSPHSHFSVI KVASIIELNT LYIDGNDNGS MNLDSLRDNL RSVQSEEDLT FIVSINFGTT
     TQAAFDDVFE IRKIFDEMKN PNWKYVVHMD AAMYGPTLPV LKQFGDKSNS LTSCGVDTVA
     ISLWKFLGVQ IPCGVSLCTR EFIKQGYEPL KATTYKDFPL ANDNFILAGT RSGIAAAAAY
     NIIKTFKLEE GLDILKKFID YDIEMAIYLQ EQLEKIYDKS EIRRMYFNVV FPRRHVPEDS
     ISKFILMKVG KTELQAITLM NVNRTLIDEF INEILAHISN NEVAQAVSE
//
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