ID A0A1Y0MQX0_9FLAO Unreviewed; 380 AA.
AC A0A1Y0MQX0;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:ARV12000.1};
GN ORFNames=BTO09_06415 {ECO:0000313|EMBL:ARV12000.1};
OS Gilvibacter sp. SZ-19.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Gilvibacter.
OX NCBI_TaxID=754429 {ECO:0000313|EMBL:ARV12000.1, ECO:0000313|Proteomes:UP000196054};
RN [1] {ECO:0000313|EMBL:ARV12000.1, ECO:0000313|Proteomes:UP000196054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SZ-19 {ECO:0000313|EMBL:ARV12000.1,
RC ECO:0000313|Proteomes:UP000196054};
RA Kumagai Y., Yoshizawa S., Kogure K., Iwasaki W.;
RT "Trade-off between light-utilization and light-protection in marine
RT flavobacteria.";
RL Submitted (DEC-2016) 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|RuleBase:RU362118};
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000256|ARBA:ARBA00009077, ECO:0000256|RuleBase:RU362118}.
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DR EMBL; CP019333; ARV12000.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0MQX0; -.
DR OrthoDB; 9803729at2; -.
DR Proteomes; UP000196054; 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:SF92; CYSTATHIONINE GAMMA-SYNTHASE; 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:UP000196054}.
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 196
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 380 AA; 41333 MW; EF8395369CC002E5 CRC64;
MKFNTKTIHG GQHEIDPAYG SVMPPIYQTS TYSQTTPGGH KGHQYARSSN PTRSALEASL
AALEDGNHAF AFGSGLAAID AVLKLLKAGD EVIATNDLYG GTYRLFTQIF EKFGVKFHFV
GMQHADKVAS YINENTKLIW VETPTNPMLN IIDIKGIATL AKANKVLLGV DNTFATPYLQ
QPLALGADIV MHSATKYLGG HSDVIMGALV VKDQELADRL YFIRNSSGAV PGPQDCFLVL
RGIKTLHLRV QRHCENGRAV AEFLRSHPKI DKVYWPGFED HPNHQVAKAQ MKDFGGMMSF
STVDDSYQGA VNVVEKLKIF TLAESLGGVE SLAGHPASMT HGSIPKAERE KTGIKDSLIR
LSVGIEDAED LIADLKQALA
//