ID   A0A091E4F5_FUKDA        Unreviewed;       654 AA.
AC   A0A091E4F5;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Histidine decarboxylase {ECO:0000256|ARBA:ARBA00039946};
DE            EC=4.1.1.22 {ECO:0000256|ARBA:ARBA00012320};
GN   ORFNames=H920_01131 {ECO:0000313|EMBL:KFO37465.1};
OS   Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC   Fukomys.
OX   NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO37465.1, ECO:0000313|Proteomes:UP000028990};
RN   [1] {ECO:0000313|EMBL:KFO37465.1, ECO:0000313|Proteomes:UP000028990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Liver {ECO:0000313|EMBL:KFO37465.1};
RA   Gladyshev V.N., Fang X.;
RT   "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT   African mole rats.";
RL   Submitted (NOV-2013) 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};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|ARBA:ARBA00009533}.
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DR   EMBL; KN120828; KFO37465.1; -; Genomic_DNA.
DR   RefSeq; XP_010636885.1; XM_010638583.1.
DR   AlphaFoldDB; A0A091E4F5; -.
DR   STRING; 885580.ENSFDAP00000003786; -.
DR   Ensembl; ENSFDAT00000017413; ENSFDAP00000003786; ENSFDAG00000013147.
DR   GeneID; 104872353; -.
DR   CTD; 3067; -.
DR   eggNOG; KOG0628; Eukaryota.
DR   OMA; MKREDSC; -.
DR   OrthoDB; 47798at2759; -.
DR   Proteomes; UP000028990; Unassembled WGS sequence.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   GO; GO:0042423; P:catecholamine biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd06450; DOPA_deC_like; 1.
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   InterPro; IPR021115; Pyridoxal-P_BS.
DR   PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR11999:SF68; HISTIDINE DECARBOXYLASE; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   PRINTS; PR00800; YHDCRBOXLASE.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE   3: Inferred from homology;
KW   Catecholamine biosynthesis {ECO:0000256|ARBA:ARBA00022584};
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028990}.
FT   MOD_RES         304
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   654 AA;  73391 MW;  FB0D296C2057FFEF CRC64;
     MEPEEYRRRG REMVDYISQY LSTVRDRRVT PDVQPGYLRE LLPESAPEEP DSWDSIFGDI
     ERVIMPGVVH WQSPHMHAYY PALTSWPSLL GDMLADAINC LGFTWASSPA CTELEMSMMD
     WLARMLGLPH HFLHGHPGSQ GGGVLQSTVS ESTLIALLAA RKNKILELQR SEPDVDESSL
     NARLVAYASD QAHSSVEKAG LISLVKMKFL PVDNNFSLRG DALQRAIEED RRRGLVPVFV
     CATLGTTGVC AFDCLSELGP VCAREGLWLH VDAAYAGTAF LCPEFRGFLQ GIEFADSFTF
     NPSKWMMVHF DCTGFWVKDK MQLQQTFGVN PVYLRHANSG STTDFMNWQI PLSRRFRSIK
     LWFVIRSFGV KNLQAHVRHG TEMAKVFESL VRNDPFFEIP AKRHLGLVVF RLKGPNCLTE
     SILKEIAKDG RLFLIPATIQ NKLIIRFTVT SQFTTKDDIL RDWNLIRDAA TLVLSQHCTS
     QPSPQTRGCS VLARGMPLQS VNKGGDDPTQ ARKIIKQPQR VGTSPVRRED SCHLETLVDP
     LDDCFSEEAP EVTKHKLSSF LFSYLSVQNK KKAVRSLSCN SVPVSAQKPF PAEGSAKNGG
     TSRVRIFSRF PEEMMLLKKS AFKKLIKFYS VPSFPECSSQ CGLQLPCCPL QAMV
//