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
//