ID A0A0S9DA84_9MICC Unreviewed; 394 AA.
AC A0A0S9DA84;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:KQO02816.1};
GN ORFNames=ASF21_00105 {ECO:0000313|EMBL:KQO02816.1};
OS Arthrobacter sp. Leaf234.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1736303 {ECO:0000313|EMBL:KQO02816.1, ECO:0000313|Proteomes:UP000053418};
RN [1] {ECO:0000313|Proteomes:UP000053418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf234 {ECO:0000313|Proteomes:UP000053418};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf234 {ECO:0000313|Proteomes:UP000053418};
RA Vorholt J.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQO02816.1}.
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DR EMBL; LMLU01000001; KQO02816.1; -; Genomic_DNA.
DR RefSeq; WP_055765156.1; NZ_LMLU01000001.1.
DR AlphaFoldDB; A0A0S9DA84; -.
DR STRING; 1736303.ASF21_00105; -.
DR Proteomes; UP000053418; 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}.
FT REGION 1..27
FT /note="Disordered"
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 394 AA; 41394 MW; B956DE1D52D147F0 CRC64;
MATDHPDLAP DTLTVAAGRP PREHDAPVNV PIVLSTTYHE TRAPQPGDRI YARGSSPTWD
PFEEALGALE GADLPALVFG SGLGAAAAAL SLVPTGGAVV MPRHAYAGSI SLAGDLAAQG
RFELLAVDIA DTDAVLGTLD ALAHRFEAGQ VMLWLESPTN PMLEVADLAV LTDAAHAHGA
LVVADNTFNT PMVHRPLEAG VDVVLHSVTK WLAGHSDVVL GALATSDAAL RGRLLAHRTL
HGAIAGPFEV WLALRGLRTL ALRMERSQST AAFLALHLAD HPAVRRVRYP GLASDPGHER
AAAQFNGFGG IVSIELDDVA TADAVVEAVR LWLPATSLGG VESLVERRRR QPAEPATVPE
ALVRLSVGIE NPEDLWADLE QALRRATGGR DGGL
//
