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Database: UniProt
Entry: A0A3Q1G0P5_9TELE
LinkDB: A0A3Q1G0P5_9TELE
Original site: A0A3Q1G0P5_9TELE 
ID   A0A3Q1G0P5_9TELE        Unreviewed;       561 AA.
AC   A0A3Q1G0P5;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Histidine decarboxylase {ECO:0000256|ARBA:ARBA00039946};
DE            EC=4.1.1.22 {ECO:0000256|ARBA:ARBA00012320};
OS   Acanthochromis polyacanthus (spiny chromis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Acanthochromis.
OX   NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000023348.1, ECO:0000313|Proteomes:UP000257200};
RN   [1] {ECO:0000313|Ensembl:ENSAPOP00000023348.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU000382};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
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DR   AlphaFoldDB; A0A3Q1G0P5; -.
DR   STRING; 80966.ENSAPOP00000023348; -.
DR   Ensembl; ENSAPOT00000011490.1; ENSAPOP00000023348.1; ENSAPOG00000005147.1.
DR   GeneTree; ENSGT00940000157938; -.
DR   InParanoid; A0A3Q1G0P5; -.
DR   Proteomes; UP000257200; Unplaced.
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   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, ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000257200}.
FT   REGION          541..561
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   561 AA;  63527 MW;  2857DEDB31EC64F8 CRC64;
     NGPEFYLLSG KELVDYITQY LSSIRERRVI PDVKPGYMKE LLPDAAPTEP EDWENIFNDI
     EKVIMPGVVH WQSPHMHAYY PSLTSWPSML GDMLADAINC VGFTWASSPA CTELEMNVMD
     WLCKALGLPS FFLHHHPDSR GGGILQSTVS ESTLVALLAA RKDKILQLRT ELEQDVDDSV
     LNSRLVAYAS DQAHSSVEKA GLISLVKIRF LPTDEQLSLR GDTLKEAIQE DRRRGLVPFM
     LCSTLGTTGV CEEEGLWLHV DAAYAGSAYF CPELRWSLQG IEFADSFVFN PSKWMMVHFD
     CTAFWVKDKY KLQQTFSVDP VYLRHENSQA ATDFMHWQIP LSRRFRSLKL WFVMRSFGLK
     NLQAHIRHKF GEFTTGRRLT RSGTMYLIPA DIHTKRIIRF TVTSQFTSAE DILKDWNIIS
     KTASALLAET QAPNNPDQPK SGEDEAIGLW IDKAWNRSRR PMRSLSCNSE PLPYSYIGPL
     SDFETRPNLK DLTKFYSVPS FCNQWVQCGR HQLCCPLKVS QGTQKHLSST CRRINCMSSS
     PVANAAPPPT PLETASAPTL L
//
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