ID Q17874_CAEEL Unreviewed; 611 AA.
AC Q17874;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 3.
DT 27-MAR-2024, entry version 149.
DE SubName: Full=Histidine Decarboxyase Like {ECO:0000313|EMBL:CAA90974.3};
GN Name=hdl-2 {ECO:0000313|EMBL:CAA90974.3,
GN ECO:0000313|WormBase:C09G9.4};
GN ORFNames=C09G9.4 {ECO:0000313|WormBase:C09G9.4}, CELE_C09G9.4
GN {ECO:0000313|EMBL:CAA90974.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CAA90974.3, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CAA90974.3, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CAA90974.3,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|ARBA:ARBA00009533}.
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DR EMBL; BX284604; CAA90974.3; -; Genomic_DNA.
DR PIR; T19152; T19152.
DR RefSeq; NP_501539.3; NM_069138.3.
DR AlphaFoldDB; Q17874; -.
DR SMR; Q17874; -.
DR STRING; 6239.C09G9.4.1; -.
DR PaxDb; 6239-C09G9-4; -.
DR EnsemblMetazoa; C09G9.4.1; C09G9.4.1; WBGene00006409.
DR GeneID; 182464; -.
DR KEGG; cel:CELE_C09G9.4; -.
DR UCSC; C09G9.4; c. elegans.
DR AGR; WB:WBGene00006409; -.
DR WormBase; C09G9.4; CE40800; WBGene00006409; hdl-2.
DR eggNOG; KOG0628; Eukaryota.
DR GeneTree; ENSGT00940000157938; -.
DR HOGENOM; CLU_474288_0_0_1; -.
DR InParanoid; Q17874; -.
DR OMA; ERIICKW; -.
DR OrthoDB; 2880688at2759; -.
DR PhylomeDB; Q17874; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00006409; Expressed in adult organism and 1 other cell type or tissue.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016831; F:carboxy-lyase activity; IBA:GO_Central.
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; 1.20.1340.10; dopa decarboxylase, N-terminal domain; 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 PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR PANTHER; PTHR11999:SF140; HISTIDINE DECARBOXYASE LIKE; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR PRINTS; PR00800; YHDCRBOXLASE.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 39..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 611 AA; 69188 MW; EC65D9406F103377 CRC64;
MGAEVPALIV CLVVSLCFNA GFIVYFVLKR KSEKVSEYKK VENPDVENFS KSSVRPPPPE
PKPQRSPPDR EKESKDPQPM NNNRSKEHVL RSENQAPTNE IQQRSDRQKL QEPIGKNEFI
KCMSLVVQFI NDYFDESHKQ PVIPENDVNS SRIHVKVPEK AEELTEILKD LKEIVIPNIC
HTHHPRYHAK FAGKSLADLV ASTISAALGH DVNSSPIIES IERIICKWLS TSMAIPQIKS
SLGELRDPIG TVFYTPCDVF ISVIRHAIEK FEKTDSGKER SKNADYIVYC SDDSQVPLKE
PCISCRVKLR KVITDEKNGS GMTSANLLKQ MEKDIARGFT PLVIIANYGS ANIAANDEIW
DLVTVSRSKK IWLHLDASYA GCEWLDSNSR NNVHALISEV HSVHITCSSL FPYSGRISVV
WSCEKLELDG AKILYGEHPI RLWILIRLHG IRSIREAVKR KIILGNAFSE RMSHHSQLFE
MHHTNEHGVT VFQYKNKKIK DRTEDTNKIT SMFHNYLVLS STLKFSIVSF HGKVLIKSVV
NYGRCNLSIM DESVSTLVNS VDEFEEALKK KKKIVCETPK NEFCEMIGGS PNETTDTTQS
DDGIDKKKKK N
//
