ID A0A1H8SFI1_9PSEU Unreviewed; 472 AA.
AC A0A1H8SFI1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Glutamate or tyrosine decarboxylase {ECO:0000313|EMBL:SEO76933.1};
GN ORFNames=SAMN04489732_10262 {ECO:0000313|EMBL:SEO76933.1};
OS Amycolatopsis saalfeldensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=394193 {ECO:0000313|EMBL:SEO76933.1, ECO:0000313|Proteomes:UP000198582};
RN [1] {ECO:0000313|EMBL:SEO76933.1, ECO:0000313|Proteomes:UP000198582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44993 {ECO:0000313|EMBL:SEO76933.1,
RC ECO:0000313|Proteomes:UP000198582};
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; FOEF01000002; SEO76933.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8SFI1; -.
DR STRING; 394193.SAMN04489732_10262; -.
DR OrthoDB; 3401800at2; -.
DR Proteomes; UP000198582; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000198582}.
FT MOD_RES 230
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 472 AA; 48855 MW; 19EEBAF3DE648D0F CRC64;
MNEVLAQLRE LRAGDLPTHG GRTLAYVYDS GLSEVDEIAA AAHALASSAN GLDPTAFPSL
LRMENDLVAT AAGLLGGDAE TVGTVTSGGT ESCLLAVLAA RDARPGLAAP GLVLAETAHA
AFHKAAHLFG VRKVVVPVDP VTFRADPAAM AAAIDESTVL VVASAPSYAH GVVDPIPEIA
AAAAARGVRM HVDGCIGAWV LPYLARLGAD VPPFDFRVPG VTSISVDLHK YAYCAKGVSV
LLHANAGLRR THYFASADWP GYTMLNPTLQ STRSGGPLAA AWAVVRHLGD EGYLRLAEVT
REAVARIRAG IEGINGLRVL GDPDSTLIAF TAAAPGFDLF TVADEMKVRG WYVQPQFAHG
SSPLNLHLTV TAANHGSEAE FLADLTASVL AAKSAGPVTV DPDVAAFVAA LDPETLTTEQ
FGDLLAAAGL TGGDGLPDRM APINALLATA AEPLRERLLL EFLGALYTPG PH
//