ID A0A099Y2Y1_9FLAO Unreviewed; 385 AA.
AC A0A099Y2Y1;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Cys/Met metabolism PLP-dependent enzyme {ECO:0000313|EMBL:KGL63198.1};
DE EC=2.5.1.48 {ECO:0000313|EMBL:KGL63198.1};
DE EC=2.5.1.49 {ECO:0000313|EMBL:KGL63198.1};
GN ORFNames=PHEL85_0231 {ECO:0000313|EMBL:KGL63198.1};
OS Polaribacter sp. Hel1_85.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1250005 {ECO:0000313|EMBL:KGL63198.1, ECO:0000313|Proteomes:UP000029991};
RN [1] {ECO:0000313|EMBL:KGL63198.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hel1_85 {ECO:0000313|EMBL:KGL63198.1};
RA Xing P., Hahnke R.L., Unfried F., Markert S., Huang S., Barbeyron T.,
RA Harder J., Becher D., Schweder T., Gloenk F.O., Amann R.I., Teeling H.;
RT "Niches of two polysaccharide-degrading Polaribacter strains isolated from
RT the North Sea during a spring diatom bloom.";
RL ISME J. 0:0-0(2014).
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 -!- 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:KGL63198.1}.
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DR EMBL; JPDS01000001; KGL63198.1; -; Genomic_DNA.
DR RefSeq; WP_036819958.1; NZ_JPDS01000001.1.
DR AlphaFoldDB; A0A099Y2Y1; -.
DR STRING; 1250005.PHEL85_0231; -.
DR eggNOG; COG0626; Bacteria.
DR OrthoDB; 9803729at2; -.
DR Proteomes; UP000029991; Unassembled WGS sequence.
DR GO; GO:0016846; F:carbon-sulfur lyase activity; IEA:UniProt.
DR GO; GO:0003962; F:cystathionine gamma-synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0102028; F:cystathionine gamma-synthase activity (acts on O-phosphohomoserine); IEA:UniProtKB-EC.
DR GO; GO:0003961; F:O-acetylhomoserine aminocarboxypropyltransferase activity; IEA:UniProtKB-EC.
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; 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 Transferase {ECO:0000313|EMBL:KGL63198.1}.
FT MOD_RES 200
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 385 AA; 42766 MW; EE3597264069EA3F CRC64;
MKESKKLGIN TTCVHVGEVK DEQFKGAVSP IYPSTSYAFD GVDVKRYPRY FNTPNQEMLH
KKIAALEKTE DALIFGSGMA AISAALFGFL QKGDHVVVQQ VIYGGTYNFI VSEFDKFGIE
YSFTESDKVE DFNALIKKNT KVLYIETPSN PLLGITDMKA ISSLAKEHAI LTMIDNTFAS
PINQNPIDFG IDIMLHSATK YMGGHSDISA GAIAASKEHI EQIWKTAINF GGNLSNQTVW
LLERSLKTLN LRVKEQTKNA QFMAEYLENN SNIDAVYYPG LKSHPQYELA KKQMKGFGAM
LSFELSEGID AMKFQNNLEL IKPSMSLAGL ESTTVSPTQT THALLSEEER LSRGIKDGLI
RFSVGIEETK DLIEDIEQAI KKAKS
//
