ID A0A0W0ZYG6_9GAMM Unreviewed; 597 AA.
AC A0A0W0ZYG6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Sphingosine-1-phosphate lyase I {ECO:0000313|EMBL:KTD74151.1};
GN ORFNames=Ltuc_1998 {ECO:0000313|EMBL:KTD74151.1};
OS Legionella tucsonensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=40335 {ECO:0000313|EMBL:KTD74151.1, ECO:0000313|Proteomes:UP000054693};
RN [1] {ECO:0000313|EMBL:KTD74151.1, ECO:0000313|Proteomes:UP000054693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49180 {ECO:0000313|EMBL:KTD74151.1,
RC ECO:0000313|Proteomes:UP000054693};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-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, 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:KTD74151.1}.
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DR EMBL; LNZA01000001; KTD74151.1; -; Genomic_DNA.
DR RefSeq; WP_058521126.1; NZ_LNZA01000001.1.
DR AlphaFoldDB; A0A0W0ZYG6; -.
DR STRING; 40335.Ltuc_1998; -.
DR PATRIC; fig|40335.7.peg.2124; -.
DR OrthoDB; 9803665at2; -.
DR Proteomes; UP000054693; 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; 2.
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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000054693}.
FT COILED 80..107
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 358
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 597 AA; 66525 MW; C16A0550EA65F920 CRC64;
MLTYITELFN SALEGFDETF KDTPAHQIVF ATAALYFLWQ QYPAIAQAYR ARNNTTYKQR
VIDTAYSLGK NLPQVKAHLD KELNKDLQST KEKLKELRAQ MALQDKIPEE STPPGLILKE
FGINPEECLF NFSGIKSDDK ARKFAVQKGD GQDSGALYAV HPQELTELLK EVYAKTALTN
PLHDKWPRII AMQAEIIRWC QELFGGSKEG YGLITHGGST SIIEAMAAYV IHARAKGIKY
PEIVVPETAH AAFKKAADLT GARLITVPVD PKTGTVTANE MKKYISSNTA VIVGSAPSFM
NGIHDPISEL GLLAQEKEVP FHVDACLGGF LTAFLDTSKN PMDFRVKGVT SISADLHKYG
CCPKGTSVCL FSDDSPALSV YAALNWSGGL YTTPGILDGS TSGARVAEIY TTLSYYGRKK
YQEISESIIA MRQRLQDRVE QLSKHNESGN KDIYIFSNPQ WSILGFRSDT LNAHLIADEL
EKRDWKLNLL QKPDGFHLCL THVHTLVEHF EDKFIHDLQE AIAAVKKYPE DKKPTGNVKV
YGTIGVLPTA VQEMVCRQYQ KARLYYEATC SKLGLFSACS KQEKEMDKPE VKNDLNP
//
