ID A0A226DH90_FOLCA Unreviewed; 877 AA.
AC A0A226DH90;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Aromatic-L-amino-acid decarboxylase {ECO:0000256|ARBA:ARBA00040968};
DE EC=4.1.1.28 {ECO:0000256|ARBA:ARBA00038886};
DE AltName: Full=DOPA decarboxylase {ECO:0000256|ARBA:ARBA00041275};
GN ORFNames=Fcan01_20871 {ECO:0000313|EMBL:OXA44224.1};
OS Folsomia candida (Springtail).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Isotomoidea; Isotomidae; Proisotominae; Folsomia.
OX NCBI_TaxID=158441 {ECO:0000313|EMBL:OXA44224.1, ECO:0000313|Proteomes:UP000198287};
RN [1] {ECO:0000313|EMBL:OXA44224.1, ECO:0000313|Proteomes:UP000198287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VU population {ECO:0000313|EMBL:OXA44224.1,
RC ECO:0000313|Proteomes:UP000198287};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXA44224.1};
RA Faddeeva A., Derks M.F., Anvar Y., Smit S., Van Straalen N., Roelofs D.;
RT "The genome of Folsomia candida.";
RL Submitted (DEC-2015) 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 -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|ARBA:ARBA00009533}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OXA44224.1}.
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DR EMBL; LNIX01000019; OXA44224.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A226DH90; -.
DR STRING; 158441.A0A226DH90; -.
DR Proteomes; UP000198287; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
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 CDD; cd14016; STKc_CK1; 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; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR010977; Aromatic_deC.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
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; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR11999:SF70; AROMATIC-L-AMINO-ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR PRINTS; PR00800; YHDCRBOXLASE.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000198287};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..877
FT /note="Aromatic-L-amino-acid decarboxylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012940316"
FT DOMAIN 81..348
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT MOD_RES 705
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 877 AA; 99018 MW; E0C6903DFC7D7531 CRC64;
MPAAAGSRFL PRLFFFLAII VFLSLPSSPS SPYEYLLVVI FMAYRISGRG ARMAAAAAPP
VEAPASSSRA DEVVVVVAGR YHLVRKIGSG SFGDIYLAYN INREGLEEVA VKIEKKKARY
PQLVFENKVY TALQGGIGIP RIHSFGQEGD YNFLVMDLLG SSLEELFNTC SRRFSMKTVL
MLADQMIARV EYIHSKNFIH RDIKPDNFLM GGGRHSSRLY LIDFGLAKKY RDPRMGQHIS
YRENKNLTGT ARYASINAHV GIEQSRRDDM ESLGYLLMYF VRGGLPWQGL KAAGKKQKYE
KIAEKKMTTP FEVLCKGYPP EFAYYFNYCR GLRFEETPDY MYLRKLFLVL FRSLGHQYDY
NFDWNKFEYK AVAPSSTAHQ QSAPPNVPYG GRLKINPHFG MDSETFLKFG EAMLKYITEY
TDNIRERRVL PTVSPGYLRP LIPSSPPDEG EPWQNIMADI ERVIMPGVTH WNSPHFHAYY
PTANSYPALV ADMLSSAIGC VGFTWIASPS CTELEIVMMD WLGKMVHLPD KFLTVESRGV
GGGMIQGTAS EANLLTLLTA RTRMVKYCKN NRKPGYDETT ILGRLVAYAS DQAHSSVERA
GLLAGVKMNL IKTDDILEMR GDALKFAIRR DKAKGLIPFY VVATLGSTNT CAFDKLSEIG
EVCAEEGVWL HVDAAYAGSA FICEEFRHLM NGVEFADSFN FNPHKWLLVN FDCSALWIAN
SKEIVDSFNV DPPCLRHASN GLIQDFRHRE IPFGRRFRSL KLWFVMRIYG LKGLQEHIRG
QTKLAHEFEK LVEKDARFEL VAPVVMGLVC FRMKDKTNEE NGKFLNAING RGKIHLVSSH
LHGKYIIRFA VCSTATASKD VAFAWKEIAD VADQLGV
//
