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
//