ID A0A061LY01_9MICO Unreviewed; 381 AA.
AC A0A061LY01;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:EYT53728.1};
GN ORFNames=H490_0110280 {ECO:0000313|EMBL:EYT53728.1};
OS Leucobacter sp. UCD-THU.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leucobacter.
OX NCBI_TaxID=1292023 {ECO:0000313|EMBL:EYT53728.1, ECO:0000313|Proteomes:UP000026917};
RN [1] {ECO:0000313|EMBL:EYT53728.1, ECO:0000313|Proteomes:UP000026917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCD-THU {ECO:0000313|EMBL:EYT53728.1,
RC ECO:0000313|Proteomes:UP000026917};
RX PubMed=23792744; DOI=10.1128/genomeA.00325-13;
RA Holland-Moritz H.E., Bevans D.R., Lang J.M., Darling A.E., Eisen J.A.,
RA Coil D.A.;
RT "Draft Genome Sequence of Leucobacter sp. Strain UCD-THU (Phylum
RT Actinobacteria).";
RL Genome Announc. 1:S69-S82(2013).
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:EYT53728.1}.
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DR EMBL; APJM01000017; EYT53728.1; -; Genomic_DNA.
DR RefSeq; WP_017884683.1; NZ_KB714603.1.
DR AlphaFoldDB; A0A061LY01; -.
DR STRING; 1292023.H490_0110280; -.
DR HOGENOM; CLU_018986_2_2_11; -.
DR OrthoDB; 9780685at2; -.
DR Proteomes; UP000026917; 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 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: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.
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:UP000026917}.
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 202
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 381 AA; 40139 MW; 56B66CF3CEAE4F7D CRC64;
MSQQAPELRS STAVVTLGRP DPTPDGPLNP PISLSSTFRS AGAPQQGERV YARYANPTWE
PLEEAIASLE GGDLPGLAFA SGMAAVSAAL SLVPVGGVAV VPSASYNGTI GLARDLAEAG
SLVLHEVDPL DLAATIAALE GADLLWLESP TNPMLDVVDL PRLVSEARRR GVTAVVDNTF
STPLRQRPLS VGADVVVHSA TKFIAGHSDV LLGLVVARNG ELRARLAKHR TLHGGIAGPF
EAWLALRGLR TMALRLDRAE ATADELARRL LEHPAVERVR YPGLPSDPNH ERARVQLDGF
GAIVSIEPSG GADAADRLVE ALGLFTPATS LGGVESLVER RRRHAAEPLE VPEALVRLSI
GIEHVEDLWA DLDRALTAAA G
//
