ID M7XJE6_9BACT Unreviewed; 418 AA.
AC M7XJE6;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=L-tyrosine decarboxylase {ECO:0000313|EMBL:EMS34683.1};
GN ORFNames=C943_03370 {ECO:0000313|EMBL:EMS34683.1};
OS Mariniradius saccharolyticus AK6.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Mariniradius.
OX NCBI_TaxID=1239962 {ECO:0000313|EMBL:EMS34683.1, ECO:0000313|Proteomes:UP000010953};
RN [1] {ECO:0000313|EMBL:EMS34683.1, ECO:0000313|Proteomes:UP000010953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK6 {ECO:0000313|EMBL:EMS34683.1,
RC ECO:0000313|Proteomes:UP000010953};
RA Vaidya B., Khatri I., Tanuku N.R.S., Subramanian S., Pinnaka A.;
RT "Genome assembly of Mariniradius saccharolyticus AK6.";
RL Submitted (JAN-2013) 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}.
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:EMS34683.1}.
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DR EMBL; AMZY02000005; EMS34683.1; -; Genomic_DNA.
DR RefSeq; WP_008624261.1; NZ_AMZY02000005.1.
DR AlphaFoldDB; M7XJE6; -.
DR STRING; 1239962.C943_03370; -.
DR eggNOG; COG0076; Bacteria.
DR InParanoid; M7XJE6; -.
DR OrthoDB; 9803665at2; -.
DR Proteomes; UP000010953; 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:UP000010953}.
FT MOD_RES 265
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 418 AA; 47723 MW; 36B6892CC66FC448 CRC64;
MYWKKQTHEQ IKETIFAALS QNLDYRGEHP ILGIPGTYLD TAEFYPDAPF LKDAPYMSAM
VRNPNHIGVH TLSEKSVLEI FEGTQKIEKD LIRLCAEEIF NGDPGQQDGY VATGGTEANI
QAMWIYRNFF RKEFGARIGE IGLVYSEDSH YSMPKGANIL NLTSIILEVD KDTREILPHS
LESKIKTAMD EGIKYFIVIA NLSTTMFGSV DDIDMLGDFF TNMNAPFKIH VDAAYGGFIY
PFTNPTSRFT FQNPYLNSIT SDGHKMLQTP YGTGLFLIRK GYFDFVKTDE AQYIPGKDYT
VSGSRSGANA ISMWMILQIH GSEGWKYKME TLCDHTERIC KRLTGMGVEF FRNPYLNIIS
IKAKYISSEL AHKYYLVANS YEFEPTWYKI VVMPHVKQGT IDSFLMDLEG ELKARQMR
//
