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Database: UniProt
Entry: A0A327ZG17_9ACTN
LinkDB: A0A327ZG17_9ACTN
Original site: A0A327ZG17_9ACTN 
ID   A0A327ZG17_9ACTN        Unreviewed;       383 AA.
AC   A0A327ZG17;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Cystathionine gamma-lyase {ECO:0000313|EMBL:RAK40300.1};
GN   ORFNames=B0I29_103332 {ECO:0000313|EMBL:RAK40300.1};
OS   Actinoplanes lutulentus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=1287878 {ECO:0000313|EMBL:RAK40300.1, ECO:0000313|Proteomes:UP000249341};
RN   [1] {ECO:0000313|EMBL:RAK40300.1, ECO:0000313|Proteomes:UP000249341}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.7090 {ECO:0000313|EMBL:RAK40300.1,
RC   ECO:0000313|Proteomes:UP000249341};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
RL   Submitted (JUN-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|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:RAK40300.1}.
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DR   EMBL; QLMJ01000003; RAK40300.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A327ZG17; -.
DR   OrthoDB; 9780685at2; -.
DR   Proteomes; UP000249341; 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: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   Lyase {ECO:0000313|EMBL:RAK40300.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000249341}.
FT   MOD_RES         203
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   383 AA;  40747 MW;  0D837D91C17FBEE2 CRC64;
     MTANQYGFDT LAIHAGQDPD PRTGAVVPPI YQTSTYAQDA VGAPRLGYEY SRSSNPTRDA
     LQECLAAIEG GRRGLAFASG LAAEDTLLRT VCRPGDHVVI PNDAYGGTYR LFAKVAERWG
     LDWTAVPLDD IDAVRAAFRP GHTRLIWAET PTNPLLNIAD IPLLAGLAHE YDALLAVDNT
     FASPYLQQPL ALGADVVIHS TTKYIGGHSD VVGGALITAD TGFGDELAFH QNAMGGVNGP
     FDAWLTLRGI KTLGVRMDRH CDNAERIAGY LSEHRAVSQV LYPGLDTHPG HEVAAKQMSR
     FGGMVSFRAA GGAEKAIEIC NRAKLFVLAE SLGGVESLIE HPGQMTHLSA AGSALEVPAD
     LVRLSVGIET VDDLLADLEQ ALG
//
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