ID A0A0M0K078_9EUKA Unreviewed; 504 AA.
AC A0A0M0K078;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Histidine decarboxylase {ECO:0000313|EMBL:KOO31972.1};
GN ORFNames=Ctob_015650 {ECO:0000313|EMBL:KOO31972.1};
OS Chrysochromulina tobinii.
OC Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Prymnesiales;
OC Chrysochromulinaceae; Chrysochromulina.
OX NCBI_TaxID=1460289 {ECO:0000313|EMBL:KOO31972.1, ECO:0000313|Proteomes:UP000037460};
RN [1] {ECO:0000313|Proteomes:UP000037460}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP291 {ECO:0000313|Proteomes:UP000037460};
RX PubMed=26397803; DOI=10.1371/journal.pgen.1005469;
RA Hovde B.T., Deodato C.R., Hunsperger H.M., Ryken S.A., Yost W., Jha R.K.,
RA Patterson J., Monnat R.J. Jr., Barlow S.B., Starkenburg S.R.,
RA Cattolico R.A.;
RT "Genome Sequence and Transcriptome Analyses of Chrysochromulina tobin:
RT Metabolic Tools for Enhanced Algal Fitness in the Prominent Order
RT Prymnesiales (Haptophyceae).";
RL PLoS Genet. 11:e1005469-e1005469(2015).
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}.
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:KOO31972.1}.
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DR EMBL; JWZX01001879; KOO31972.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M0K078; -.
DR OrthoDB; 750275at2759; -.
DR Proteomes; UP000037460; 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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; 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 PANTHER; PTHR46101; -; 1.
DR PANTHER; PTHR46101:SF2; SERINE DECARBOXYLASE; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 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:UP000037460}.
FT MOD_RES 333
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 504 AA; 56138 MW; A2C315721DE22453 CRC64;
MCSTALRGLS SVASGLVRRQ SAWPLHLHVR NAITLRRDFC ARANAAHALD DASSEKLGSA
SPWATDGWGD SVEIIEQTMP DAHRALLSNA SVAIPTSSAE AGELPAVSDI LGAYEAQLQR
RTARHLGYPY NLDYQNRELD RFMRYSINNL GDPFVPSNYG VHSRQFEVAV VDFFARLWRA
DPNDYWGYVT TCGTEGNLYG MLLARETLPD GIVYTSSETH YSVFKAAHYY RQEVEVIPTL
FNGQIDYDAL ATALRRNRGK PAILNVNIGT TVKGAVDDLD RILRTLSMTG YEREDYYVHC
DGALFAMMMP FVEYAPELSF QRPIDSITVS GHKMLGCPMP CGIALTRRSH VRKIERRIDY
LNSVDTTIMG SRNGHAALHM WHSLRTKGLE GIKAEVASCL KTAVYLRDSL SAEGITCQLN
DLSSTVILER PADERFVKRW QLACEEDIAH VVVMPNVTTK KVDIFVAELV AMTKQHGRTA
PRRENSPLTL LSSKAWGAHR AGHA
//
