ID A0A3B4TEM1_SERDU Unreviewed; 675 AA.
AC A0A3B4TEM1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Histidine decarboxylase {ECO:0000256|ARBA:ARBA00039946};
DE EC=4.1.1.22 {ECO:0000256|ARBA:ARBA00012320};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000004470.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000004470.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 AlphaFoldDB; A0A3B4TEM1; -.
DR STRING; 41447.ENSSDUP00000004470; -.
DR Ensembl; ENSSDUT00000004564.1; ENSSDUP00000004470.1; ENSSDUG00000003241.1.
DR GeneTree; ENSGT00940000157938; -.
DR Proteomes; UP000261420; 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 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}.
FT REGION 478..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 656..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..517
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 306
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 675 AA; 75704 MW; AA2FCD8D50E9C51D CRC64;
KMQAEEYNRR GKELVDYITQ YLGSIRERRV IPDVKPGYMK ELLPDTAPTE PEDWETIFND
IEKVVMPGVV HWQSPHMHAY YPSLTSWPSM LGDMLADAIN CVGFTWASSP ACTELEMNVM
DWLCKALGLP SFFLHQHPDS RGGGILQSTV SESTLVALLA ARKDKILQLR AELDQEVDDS
VLNSRLVAYA SDQAHSSVEK AGLISLVKIR FLPTDEQLSL RGDTLKQAIQ EDRRMGLVPF
MLCATLGTTG VCAFDKLSEL GPVCAEEGLW LHVDAAYAGS AYFCPELRWS LEGIDFAHSF
VFNPSKWMMV HFDCTAFWVK DKYKLQQTFS VDPVYLRHEN SQAATDFMHW QIPLSRRFRS
LKLWFVMRSF GLKNLQAHIR HGIEMAKLLE SHIRRDPNFE VPAARHLGLV VFCLKGGNAL
TQELLRRLTR SGTMYLIPAD IHTTRIIRFT VTSQFTTADD ILKDWGIISK TASTLLAETQ
GPNNSDQSKA GEDDVMEAEE NQDPNSDTRS DEKEDAASML DKAQVELWID KAWNRSRRPM
RSLSCNSEPL PYTYVGPLSG YDFDTRPALK DGAGALPTPS TPASSPLTKV TEMPSNLLGK
QVLKKLTKFY SVPSFCNQWV QCGRHPLCCP LKVSQAAQKH LSSTCRRMNC MSSSPIANTA
PSPTPLETAT APKLL
//