ID A0A0P7YY23_9RHOB Unreviewed; 391 AA.
AC A0A0P7YY23;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:KPP95870.1};
DE EC=2.5.1.48 {ECO:0000313|EMBL:KPP95870.1};
GN Name=metB {ECO:0000313|EMBL:KPP95870.1};
GN ORFNames=HLUCCA05_04150 {ECO:0000313|EMBL:KPP95870.1};
OS Roseibaca calidilacus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Roseibaca.
OX NCBI_TaxID=1666912 {ECO:0000313|EMBL:KPP95870.1, ECO:0000313|Proteomes:UP000050413};
RN [1] {ECO:0000313|EMBL:KPP95870.1, ECO:0000313|Proteomes:UP000050413}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL-91 {ECO:0000313|EMBL:KPP95870.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-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|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:KPP95870.1}.
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DR EMBL; LJSG01000002; KPP95870.1; -; Genomic_DNA.
DR RefSeq; WP_072247609.1; NZ_FBYC01000004.1.
DR AlphaFoldDB; A0A0P7YY23; -.
DR STRING; 1666912.Ga0058931_1845; -.
DR PATRIC; fig|1666912.4.peg.1984; -.
DR OrthoDB; 9805807at2; -.
DR Proteomes; UP000050413; Unassembled WGS sequence.
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:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019346; P:transsulfuration; IEA:InterPro.
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:SF90; 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.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Transferase {ECO:0000313|EMBL:KPP95870.1}.
FT MOD_RES 204
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 391 AA; 41273 MW; 7BFDDC9EE532267A CRC64;
MSEHESLVRR MGWPESVSRA VGTPIQPSVV YASPDPDTLD AQYEGRAQGY TYAREGHPNA
DVLARKIDQM EGATGGVVLG SGMAAVAAVL MGLTRAGDHV LGGDQLYGRS LRLMREDLPR
LGVATSLADP TDAAAFLAAL RPETKLILLE VVSNPTLRVA DLAAIIDGAQ ARGVLVVVDN
TFTTPRGYRP FDHGADIVVH SVTKMLAGHS DATLGYVAAR DASHRKAIYD FAVTVGFTPS
PFDCWLAERG LYSFELRYDR AEANAAALAD HIAGLPGVSR VLYPTRPDHP DHNRAVALLG
ARGGHMVSFE IGGGRAAANR LTQAAPNIAF APTLGDIGTT LSHPASSSHR ALGPEGRAAL
GISEGFFRVS VGVEDIGMLC SEFETAIRAA T
//
