ID A0A1Q5CVU9_9ACTN Unreviewed; 380 AA.
AC A0A1Q5CVU9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:OKI87699.1};
GN ORFNames=A6A27_14725 {ECO:0000313|EMBL:OKI87699.1};
OS Micromonospora sp. CB01531.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1718947 {ECO:0000313|EMBL:OKI87699.1, ECO:0000313|Proteomes:UP000186700};
RN [1] {ECO:0000313|EMBL:OKI87699.1, ECO:0000313|Proteomes:UP000186700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB01531 {ECO:0000313|EMBL:OKI87699.1,
RC ECO:0000313|Proteomes:UP000186700};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKI87699.1}.
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DR EMBL; LWLS01000002; OKI87699.1; -; Genomic_DNA.
DR RefSeq; WP_073832864.1; NZ_LWLS01000002.1.
DR AlphaFoldDB; A0A1Q5CVU9; -.
DR STRING; 1718947.A6A27_14725; -.
DR OrthoDB; 9780685at2; -.
DR Proteomes; UP000186700; 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:UP000186700}.
FT MOD_RES 200
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 380 AA; 39912 MW; 9EFC8ABB40BAB31B CRC64;
MSHGFETLAI HAGQDPEART GAVIPPIYQT STYAQDAVGA PRQGYEYSRS GNPTRDALQE
CLAALEGGPV GLAFASGLAA EDTLLRTVCK PGDHVVIPDD AYGGTYRLFA RVAERWGLSY
TPAKVSDPDA VRAAIRPGAT KIVWVETPTN PLLGIADIAA LAAVAHDAEA LLVVDNTFAS
PYLQQPIAHG ADVVVHSTTK YIGGHSDVVG GALVVADTGL GDELRYHQNA MGAVNGPFDA
WLTLRGIKTL GVRMDRHCDN AERIAAYLDG HAKVGEVLYP GLPAHPGHEV AAKQMRRFGG
MISFRAAGGE EHAVAICNRA KLFVLAESLG GVESLIEHPG RMTHASAAGS PLEVPGDLVR
LSVGIETVDD LLADLEQALG
//
