ID A6GWJ4_FLAPJ Unreviewed; 382 AA.
AC A6GWJ4;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Cys/Met metabolism PLP-dependent enzyme {ECO:0000313|EMBL:CAL42467.1};
GN OrderedLocusNames=FP0354 {ECO:0000313|EMBL:CAL42467.1};
OS Flavobacterium psychrophilum (strain ATCC 49511 / DSM 21280 / CIP 103535 /
OS JIP02/86).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=402612 {ECO:0000313|EMBL:CAL42467.1, ECO:0000313|Proteomes:UP000006394};
RN [1] {ECO:0000313|EMBL:CAL42467.1, ECO:0000313|Proteomes:UP000006394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49511 / DSM 21280 / CIP 103535 / JIP02/86
RC {ECO:0000313|Proteomes:UP000006394};
RX PubMed=17592475; DOI=10.1038/nbt1313;
RA Duchaud E., Boussaha M., Loux V., Bernardet J.F., Michel C., Kerouault B.,
RA Mondot S., Nicolas P., Bossy R., Caron C., Bessieres P., Gibrat J.F.,
RA Claverol S., Dumetz F., Le Henaff M., Benmansour A.;
RT "Complete genome sequence of the fish pathogen Flavobacterium
RT psychrophilum.";
RL Nat. Biotechnol. 25:763-769(2007).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU362118};
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000256|RuleBase:RU362118}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM398681; CAL42467.1; -; Genomic_DNA.
DR RefSeq; WP_011962525.1; NC_009613.3.
DR RefSeq; YP_001295285.1; NC_009613.3.
DR AlphaFoldDB; A6GWJ4; -.
DR STRING; 402612.FP0354; -.
DR EnsemblBacteria; CAL42467; CAL42467; FP0354.
DR GeneID; 66551489; -.
DR KEGG; fps:FP0354; -.
DR PATRIC; fig|402612.5.peg.366; -.
DR eggNOG; COG0626; Bacteria.
DR HOGENOM; CLU_018986_2_0_10; -.
DR OrthoDB; 9803729at2; -.
DR Proteomes; UP000006394; Chromosome.
DR GO; GO:0016846; F:carbon-sulfur lyase activity; IEA:UniProt.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR CDD; cd00614; CGS_like; 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; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11808:SF15; CYSTATHIONINE GAMMA-LYASE; 1.
DR PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR PIRSF; PIRSF001434; CGS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000006394}.
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 197
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 382 AA; 41909 MW; E5C8DF82C667B3F8 CRC64;
MKFNTKVIHG GQHHDPSTGA VMPPVYQTST FVQTSPGQPL NPDYEYSRAA NPTRSALENA
LASIENGTRG LAFSSGLAAT DCVLRSFKAG DEIIAMDDLY GGTYRMFTRI YANSGIKFHF
VDMNDLENFE SLINENTKLV WVETPTNPLM KIADIAEIAK ITKKHKILFA VDNTFATPYL
QKPLDLGADI VMHSATKYLG GHSDVIAGAL IVKDEELGSQ LHFQQFATGA TLGPMDSFLV
LRGIKTLHLR VQRHCENGAK VAEFLLNHSK IEKVYYPGLP SHPYHDIAKK QMIGGFGGMV
TFTFKSGKKE EAISFLEKVK VFTLAESLGG VESLANHPAL MTHASIPEDK RKEIGITDDL
VRLSVGVEDA EDLIADLKQA LL
//
