ID F5SY04_9GAMM Unreviewed; 385 AA.
AC F5SY04;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=Putative decarboxylase {ECO:0000313|EMBL:EGL54072.1};
GN ORFNames=MAMP_00206 {ECO:0000313|EMBL:EGL54072.1};
OS Methylophaga aminisulfidivorans MP.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Methylophaga.
OX NCBI_TaxID=1026882 {ECO:0000313|EMBL:EGL54072.1, ECO:0000313|Proteomes:UP000003544};
RN [1] {ECO:0000313|EMBL:EGL54072.1, ECO:0000313|Proteomes:UP000003544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP(T) {ECO:0000313|Proteomes:UP000003544};
RX PubMed=21685284; DOI=10.1128/JB.05403-11;
RA Han G.H., Kim W., Chun J., Kim S.W.;
RT "Draft genome sequence of Methylophaga aminisulfidivorans MP T.";
RL J. Bacteriol. 193:4265-4265(2011).
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.
CC {ECO:0000256|RuleBase:RU000382}.
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:EGL54072.1}.
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DR EMBL; AFIG01000001; EGL54072.1; -; Genomic_DNA.
DR RefSeq; WP_007143958.1; NZ_AFIG01000001.1.
DR AlphaFoldDB; F5SY04; -.
DR STRING; 1026882.MAMP_00206; -.
DR eggNOG; COG0076; Bacteria.
DR OrthoDB; 9803665at2; -.
DR Proteomes; UP000003544; 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; 3.40.640.10; 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 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:UP000003544}.
FT MOD_RES 241
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 385 AA; 43247 MW; D64EA62919D7DD6C CRC64;
MKNPESPVVH RSEDKQYIID TQRLMSSDIS YQDLVNEASY HQRADWAAHM TPSLAPYSQL
GMQLALHHHG NLLSPELYPK LKHAESEIKT TLAHEFGFSH ARFTHGGSYS NLDALWRARS
QSVNKKVVYG SEASHYSIRK ACDILGITFE AIPCNTAQQI DLVALEKKCA QDAPIAIIAN
MGTSATGAID PIEEITAIST KHNCWLHIDA AWGGSNLLID ENNLFKQFMP KVDSLSFDPH
KSLFQPRPCS VLFSHSKPEH THDINYLSES PEKAISGSYG AELFIPLWLN WKILGKDWFI
DKINYRLEQA EYFASQLQKQ TKWPIINHGT GIVCFKADHD ALLAPLVEKG TVSTINLNQT
CYHRVIFAGL DTSAEKLLKA LHPFL
//
