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Database: UniProt
Entry: A0A1C6N6W1_9ACTN
LinkDB: A0A1C6N6W1_9ACTN
Original site: A0A1C6N6W1_9ACTN 
ID   A0A1C6N6W1_9ACTN        Unreviewed;       388 AA.
AC   A0A1C6N6W1;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:SCK26651.1};
GN   ORFNames=H180DRAFT_02043 {ECO:0000313|EMBL:SCK26651.1};
OS   Streptomyces sp. WMMB 322.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1286821 {ECO:0000313|EMBL:SCK26651.1, ECO:0000313|Proteomes:UP000182082};
RN   [1] {ECO:0000313|EMBL:SCK26651.1, ECO:0000313|Proteomes:UP000182082}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WMMB 322 {ECO:0000313|EMBL:SCK26651.1,
RC   ECO:0000313|Proteomes:UP000182082};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) 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}.
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DR   EMBL; FMHI01000005; SCK26651.1; -; Genomic_DNA.
DR   RefSeq; WP_055485716.1; NZ_FMHI01000005.1.
DR   AlphaFoldDB; A0A1C6N6W1; -.
DR   STRING; 1286821.GCA_001418285_02034; -.
DR   OrthoDB; 9780685at2; -.
DR   Proteomes; UP000182082; 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:0009058; P:biosynthetic process; IEA:UniProt.
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}.
FT   MOD_RES         208
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   388 AA;  40944 MW;  60386AD0CC84E65F CRC64;
     MSDQRDSGHT PQSFETLAIH AGQTADPATG AVVPPIYQVS TYKQDGVGGL RGGYEYSRSA
     NPTRTALEQN LAALEGGRNA FAFASGLAAE DCLLRTLLVP GDHVVVPNDA YGGTFRLFSR
     VAERWGVEWS VADTSDPAAV RAALRDRTKA VWVETPSNPL LGISDITALA QLAHGAGARL
     VVDNTFASPY LQQPLALGAD VVVHSTTKYM GGHSDVVGGA LVLDESELAA EIAFHQNAMG
     AVAGPFDSWL VMRGTKTLAV RMERHSANAS RVAEMLQAHP RVTQVYYPGL PSHPGHETAA
     KQMRAFGGMV SFRVADGEEA AVQVCNRAQL FTLGESLGGV ESLIEHPARM THASAAGSAL
     EVPADLVRLS VGIESVEDLL ADLQQALG
//
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