ID A0A1G7RR36_9ACTN Unreviewed; 426 AA.
AC A0A1G7RR36;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Glutamate or tyrosine decarboxylase {ECO:0000313|EMBL:SDG12679.1};
GN ORFNames=SAMN05660662_0428 {ECO:0000313|EMBL:SDG12679.1};
OS Blastococcus aurantiacus.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Blastococcus.
OX NCBI_TaxID=1550231 {ECO:0000313|EMBL:SDG12679.1, ECO:0000313|Proteomes:UP000199406};
RN [1] {ECO:0000313|EMBL:SDG12679.1, ECO:0000313|Proteomes:UP000199406}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44268 {ECO:0000313|EMBL:SDG12679.1,
RC ECO:0000313|Proteomes:UP000199406};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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, ECO:0000256|RuleBase:RU000382};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family. Sphingosine-
CC 1-phosphate lyase subfamily. {ECO:0000256|ARBA:ARBA00038302}.
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DR EMBL; FNBT01000012; SDG12679.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7RR36; -.
DR STRING; 1550231.SAMN05660662_0428; -.
DR Proteomes; UP000199406; Unassembled WGS sequence.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProt.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR Gene3D; 6.10.140.2150; -; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
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 PANTHER; PTHR42735; -; 1.
DR PANTHER; PTHR42735:SF6; SPHINGOSINE-1-PHOSPHATE LYASE 1; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382}.
FT REGION 404..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 247
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 426 AA; 45648 MW; 92AE8AABE7EAB213 CRC64;
MTAARPASAE LPAQSTGAAH VLAELRANRH DDADWRNGRI FGLIFHPDDD ELEELLADVS
REYLAENALN PVRFPSLARL EREAADMVAG LLHGTPGAGG LTSGGTESIF MSVLVARETA
RKKGIADPVL VTGITAHPAF AKACHLLGMR QIRVPVDEGY RLVVEEMRAA VGPDTAMVVA
SAPCYPYGVM DPVEEVAAIA REAGVLCHVD ACLGGMMLPF WERLGEPVPP WDFRVEGVTS
ISADLHKYGY AFKGASVLLH RDVEQYRTQW WFDDGAWGGG LYGSPTAAGT RPAPPIAGAW
AALRHLGEDG YLRQATKVRD ATRRLMSGIE AIDGLSITST PDLCVFQFGS DVLDMKVVAD
ALAEQGWFPN RQPGGLHLMV SPFHVRVADD FLAALAVAVD RARDGATSDS GPAVYGAALP
SRERSA
//
