ID A0A2N0ZI95_9BACI Unreviewed; 378 AA.
AC A0A2N0ZI95;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:PKG29230.1};
DE EC=2.5.1.48 {ECO:0000313|EMBL:PKG29230.1};
GN ORFNames=CWS20_09575 {ECO:0000313|EMBL:PKG29230.1};
OS Cytobacillus horneckiae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Cytobacillus.
OX NCBI_TaxID=549687 {ECO:0000313|EMBL:PKG29230.1, ECO:0000313|Proteomes:UP000233343};
RN [1] {ECO:0000313|EMBL:PKG29230.1, ECO:0000313|Proteomes:UP000233343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1PO1SC {ECO:0000313|Proteomes:UP000233343};
RX PubMed=19666815; DOI=10.1099/ijs.0.008979-0;
RA Vaishampayan P., Probst A., Krishnamurthi S., Ghosh S., Osman S.,
RA McDowall A., Ruckmani A., Mayilraj S., Venkateswaran K.;
RT "Bacillus horneckiae sp. nov., isolated from a spacecraft-assembly clean
RT room.";
RL Int. J. Syst. Evol. Microbiol. 60:1031-1037(2010).
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}.
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:PKG29230.1}.
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DR EMBL; PISD01000018; PKG29230.1; -; Genomic_DNA.
DR RefSeq; WP_066191886.1; NZ_PISD01000018.1.
DR AlphaFoldDB; A0A2N0ZI95; -.
DR STRING; 549687.GCA_001636335_02145; -.
DR Proteomes; UP000233343; 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: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:UP000233343};
KW Transferase {ECO:0000313|EMBL:PKG29230.1}.
FT MOD_RES 195
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 378 AA; 40938 MW; F43FB886989305A7 CRC64;
MRRKTKLIHG GIVGDPATGA VSVPIYQVST YKQDGVGNHK GFEYSRTGNP TRHALEELIK
DLEGGKAGFA FGSGMAAITA VIMMFDSGDH VILTDDVYGG TYRVITKVLN RFGIEATFVD
SSDLKNIKEA IKSNTKAVYI ETPTNPLLKI TDIEAAANLA KENGLLTIVD NTFSTPYWQT
PIELGADIVL HSATKYLGGH SDVVAGLVVV NSDQLAEDLH FVQNSTGGVL GPQDSWLLMR
GIKTLGIRME ETERNTKAIV EFLLGHPAVR NVYYPGIETH PNHDIAKKQA QGFGGMVSFD
VGSEKNADQL LEGVKYFTLA ESLGAVESLI SVPARMTHAS IPKERRDELG ITDGLVRISV
GLEDAEDLIE DLKQALDN
//
