ID G3HGG5_CRIGR Unreviewed; 447 AA.
AC G3HGG5;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=H671_1g1863 {ECO:0000313|EMBL:ERE90132.1}, I79_009692
GN {ECO:0000313|EMBL:EGW07730.1};
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029 {ECO:0000313|EMBL:EGW07730.1, ECO:0000313|Proteomes:UP000001075};
RN [1] {ECO:0000313|Proteomes:UP000001075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
RX PubMed=21804562; DOI=10.1038/nbt.1932;
RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA Famili I., Palsson B.O., Wang J.;
RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL Nat. Biotechnol. 29:735-741(2011).
RN [2] {ECO:0000313|EMBL:EGW07730.1}
RP NUCLEOTIDE SEQUENCE.
RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA Fan C.H., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA Famili I., Palsson B.O., Wang J.;
RT "The genomic sequence of the Chinese hamster ovary CHO-K1 cell line.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000030759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17A/GY {ECO:0000313|Proteomes:UP000030759};
RX PubMed=23929341; DOI=10.1038/nbt.2645;
RA Brinkrolf K., Rupp O., Laux H., Kollin F., Ernst W., Linke B., Kofler R.,
RA Romand S., Hesse F., Budach W.E., Galosy S., Muller D., Noll T.,
RA Wienberg J., Jostock T., Leonard M., Grillari J., Tauch A., Goesmann A.,
RA Helk B., Mott J.E., Puhler A., Borth N.;
RT "Chinese hamster genome sequenced from sorted chromosomes.";
RL Nat. Biotechnol. 31:694-695(2013).
RN [4] {ECO:0000313|EMBL:ERE90132.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=17A/GY {ECO:0000313|EMBL:ERE90132.1};
RA Brinkrolf K., Rupp O., Laux H., Kollin F., Ernst W., Linke B., Kofler R.,
RA Romand S., Hesse F., Budach W.E., Galosy S., Muller D., Noll T.,
RA Wienberg J., Jostock T., Leonard M., Grillari J., Tauch A., Goesmann A.,
RA Helk B., Mott J.E., Puehler A., Borth N.;
RT "Chinese hamster genome sequenced from sorted chromosomes.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine
CC (DOPA) to dopamine and L-5-hydroxytryptophan to serotonin.
CC {ECO:0000256|ARBA:ARBA00037256}.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC -!- PATHWAY: Catecholamine biosynthesis; dopamine biosynthesis; dopamine
CC from L-tyrosine: step 2/2. {ECO:0000256|ARBA:ARBA00037889}.
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 EMBL; JH000349; EGW07730.1; -; Genomic_DNA.
DR EMBL; KE664266; ERE90132.1; -; Genomic_DNA.
DR AlphaFoldDB; G3HGG5; -.
DR STRING; 10029.G3HGG5; -.
DR PaxDb; 10029-XP_007634784-1; -.
DR eggNOG; KOG0628; Eukaryota.
DR InParanoid; G3HGG5; -.
DR Proteomes; UP000001075; Unassembled WGS sequence.
DR Proteomes; UP000030759; Unassembled WGS sequence.
DR GO; GO:0004058; F:aromatic-L-amino-acid decarboxylase activity; IEA:UniProtKB-EC.
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:SF70; AROMATIC-L-AMINO-ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE 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|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000001075}.
FT MOD_RES 303
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 447 AA; 49577 MW; 24F8BC112921A504 CRC64;
MDSSEFRRRG KEMVDYIADY LEGIEGRAVY PDVEPGYLRP LIPTAAPQEP DAYEDIIKDI
EKIIMPGVTH WHSPYFFAYF PTASSYPAML ADMLCGAIGC IGFTWAASPA CTELETVMMD
WLGKMLELPE AFLAGRTGEG GGVIQGSASE ATLVALLAAR TKVIRQLQAA SPELTQAAIM
EKLVAYTSDQ AHSSVERAGL IGGVKLKTIP SDGNFSMRAS ALQEALEQDK AAGLIPFFVV
VTLGTTSCCS FDNLLEVGPI CNLEGVWLHI DAAYAGSAFI CPEFRYLLNG VEFADSFNFN
PHKWLLVNFD CSAMWVKKRT DLTGAFKLDP VYLKHDHQDS GLITDYRHVA LSHEFESLVR
QDPRFEICTE VILGLVCFRL KGSNQLNETL LQRINSAKKI HLVPCHLRDK FVLRFAVCSR
TVESAHVQLA WEHIRELASS VLRAEKE
//
