ID A0A127AZ70_9BACT Unreviewed; 379 AA.
AC A0A127AZ70;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:AMM50317.1};
GN ORFNames=TH61_02765 {ECO:0000313|EMBL:AMM50317.1};
OS Rufibacter sp. DG15C.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Rufibacter.
OX NCBI_TaxID=1379909 {ECO:0000313|EMBL:AMM50317.1, ECO:0000313|Proteomes:UP000070672};
RN [1] {ECO:0000313|EMBL:AMM50317.1, ECO:0000313|Proteomes:UP000070672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG15C {ECO:0000313|EMBL:AMM50317.1,
RC ECO:0000313|Proteomes:UP000070672};
RA Kim M.K., Srinivasan S., Lee J.-J.;
RT "Rufibacter sp. DG15C whole genome sequencing.";
RL Submitted (JAN-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|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; CP010776; AMM50317.1; -; Genomic_DNA.
DR RefSeq; WP_066505588.1; NZ_CP010776.1.
DR AlphaFoldDB; A0A127AZ70; -.
DR STRING; 1379909.TH61_02765; -.
DR KEGG; rud:TH61_02765; -.
DR PATRIC; fig|1379909.4.peg.600; -.
DR OrthoDB; 634606at2; -.
DR Proteomes; UP000070672; Chromosome.
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:UP000070672}.
FT MOD_RES 195
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 379 AA; 41705 MW; 0FECB89F5E09BD9E CRC64;
MKFGTKTIHA GVEPDPTTGA IMTPIYQTST YVQRSPGDHK GYEYSRTHNP TRTALQNALA
ALENGNHGLC FASGMAATDC IIKLLKPGDE VISTNDLYGG TYRIFTKVYQ NYGIKFTFVS
MADIQSIEQH ITENTKMIWV ETPTNPLLNI IDIKGAAAIS KKHNLTLVVD NTFSTPYLQT
PLDLGADIVM HSLTKYMAGH SDVVMGAIVV KDDALAEQLA FFQNACGGTP GPQDCFLVLR
GIKTLHIRMQ RHCENGKVIA EYLRQHPKVE KVFWPGFESH PNHQIARDQM RDFGGMISFV
LKGDRQEDAI QVLEKLKYFA LAESLGGVES LCGHPATMTH ASIPQVERLK GGLSDSLIRL
SVGIEDVEDL VADLEQAIG
//