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Database: UniProt
Entry: A0A0H2KQG6_9MICO
LinkDB: A0A0H2KQG6_9MICO
Original site: A0A0H2KQG6_9MICO 
ID   A0A0H2KQG6_9MICO        Unreviewed;       413 AA.
AC   A0A0H2KQG6;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:KLN35413.1};
GN   ORFNames=FB00_06475 {ECO:0000313|EMBL:KLN35413.1};
OS   Cellulosimicrobium funkei.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC   Promicromonosporaceae; Cellulosimicrobium.
OX   NCBI_TaxID=264251 {ECO:0000313|EMBL:KLN35413.1, ECO:0000313|Proteomes:UP000035265};
RN   [1] {ECO:0000313|EMBL:KLN35413.1, ECO:0000313|Proteomes:UP000035265}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U11 {ECO:0000313|EMBL:KLN35413.1,
RC   ECO:0000313|Proteomes:UP000035265};
RA   Hu C., Gong Y., Wan W., Jiang M.;
RT   "Cellulosimicrobium funkei U11 genome.";
RL   Submitted (MAY-2014) 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:KLN35413.1}.
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DR   EMBL; JNBQ01000004; KLN35413.1; -; Genomic_DNA.
DR   RefSeq; WP_047232062.1; NZ_JNBQ01000004.1.
DR   AlphaFoldDB; A0A0H2KQG6; -.
DR   STRING; 264251.FB00_06475; -.
DR   PATRIC; fig|264251.5.peg.1321; -.
DR   Proteomes; UP000035265; 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   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035265}.
FT   MOD_RES         220
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   413 AA;  42285 MW;  C6EB6C0ACDAD6532 CRC64;
     MTTSSEHPDW TTTGFSTRAI HAGQDPDATT GAVVPPIHQV STYKQDGVGG LRGGYEYSRS
     ANPTRTALEE ALAAAESGGL RPTADGSPAA RGFAFASGLA AEDTLLRAVV RPGDHVIVPD
     DAYGGTYRLI ARVFGPWGVE HTPVDLTDVE AVRAAVRPET RVVWVETPTN PLLGVSDIAA
     LAGVAHDAGA LLVVDNTFAT PYLQQPLALG ADVVVHSTTK YVGGHSDVVG GALVVASGAQ
     LPGGLASPAG GTDVAGAVGF HQNASGAIAG PFDAWLTLRG LKTLAVRMDR HQANAAAVAD
     FLAAHPAVTE VIYPGLASHP GHELAARQMS GFGGMVSFRA GSEAKALDVC ARTQVFALAE
     SLGGVESLIE HPGRMTHGSV AGTALEVPDD LVRLSVGIED VEDLVADLTQ ALA
//
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