ID A0A3N2JJL9_9CELL Unreviewed; 407 AA.
AC A0A3N2JJL9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:ROS73558.1};
GN ORFNames=EDF32_2410 {ECO:0000313|EMBL:ROS73558.1};
OS Cellulomonas sp. PhB143.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=2485186 {ECO:0000313|EMBL:ROS73558.1, ECO:0000313|Proteomes:UP000276333};
RN [1] {ECO:0000313|EMBL:ROS73558.1, ECO:0000313|Proteomes:UP000276333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PhB143 {ECO:0000313|EMBL:ROS73558.1,
RC ECO:0000313|Proteomes:UP000276333};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-V): Genome sequencing
RT to study the core and pangenomes of soil and plant-associated
RT prokaryotes.";
RL Submitted (NOV-2018) 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:ROS73558.1}.
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DR EMBL; RKIJ01000014; ROS73558.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N2JJL9; -.
DR OrthoDB; 4966611at2; -.
DR Proteomes; UP000276333; Unassembled WGS sequence.
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 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:SF93; CYSTATHIONINE GAMMA-LYASE-RELATED; 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 Reference proteome {ECO:0000313|Proteomes:UP000276333}.
FT REGION 388..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..407
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 210
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 407 AA; 42835 MW; B77D63D7674DC6FC CRC64;
MDPARTPEHE PLPRGLSPAT VAVAAGRPLR RQGGPVNPPV VLSSTYVSQG VQGPGELLYT
RMDTETWHPF EEALAALEGA AQPAVVFSSG MAAIASVFAD VPAGGTVVVP RHAYQVTLGF
ADDLAARTGV SVRRVDVADT EQVLAALDGA DLLLVESPTN PMLEVADLPV LLAAARERGI
RSAVDNTFAT PLGQQPLALG ADLVVHSVTK YLAGHSDVVL GAVVTDDADL ARRTRAYRTL
HGSIAGPWEV WLALRGMRTL ALRVERSQAT AAELARRLAE HPAVAEVRHP SLPDDPGHER
AARTMRGFGS VLGLRPRGGV EAADALVAAV RLWLPATSLG GVESCLERRR RFATESGTVP
EDLLRMSVGI EDVEDLWADL AQALGALGAG DGHDGDDDGH SENEGAR
//
