GenomeNet

Database: UniProt
Entry: A0A0M9XAR7_9ACTN
LinkDB: A0A0M9XAR7_9ACTN
Original site: A0A0M9XAR7_9ACTN 
ID   A0A0M9XAR7_9ACTN        Unreviewed;       385 AA.
AC   A0A0M9XAR7;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:KOT44133.1};
GN   ORFNames=ADK41_04455 {ECO:0000313|EMBL:KOT44133.1};
OS   Streptomyces caelestis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=36816 {ECO:0000313|EMBL:KOT44133.1, ECO:0000313|Proteomes:UP000037773};
RN   [1] {ECO:0000313|EMBL:KOT44133.1, ECO:0000313|Proteomes:UP000037773}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-24567 {ECO:0000313|EMBL:KOT44133.1,
RC   ECO:0000313|Proteomes:UP000037773};
RA   Noorani M.;
RL   Submitted (JUL-2015) 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:KOT44133.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LGCN01000040; KOT44133.1; -; Genomic_DNA.
DR   RefSeq; WP_030830337.1; NZ_LGCN01000040.1.
DR   AlphaFoldDB; A0A0M9XAR7; -.
DR   PATRIC; fig|36816.3.peg.951; -.
DR   OrthoDB; 9780685at2; -.
DR   Proteomes; UP000037773; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037773}.
FT   MOD_RES         204
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   385 AA;  40699 MW;  DD33803ABD382437 CRC64;
     MSDRHISQHF ETLAIHAGNT ADPLTGAVVP PIYQVSTYKQ DGVGGLRGGY EYSRSANPTR
     TALEENLAAL EGGRRGLAFA SGLAAEDCLL RTLLGPGDHV VIPNDAYGGT FRLFAKVVAR
     WGVAWSVADT SDPAAVRAAI TPNTKVVWVE TPSNPLLGIT DIAAVAQVTR DAGARLVVDN
     TFATPYLQQP LALGADVVVH SLTKYMGGHS DVVGGALITG DAELGEELAY HQNAMGAVAG
     PFDSWLVLRG TKTLSVRMDR HSENATRIAD MLTRHPRVTS VLYPGLPDHP GHEVAAKQMR
     AFGGMVSFRV EGGEEAAVEV CDRAEVFTLG ESLGGVESLI EHPGRMTHAS AAGSALEVPA
     DLVRLSVGIE NVDDLLEDLQ QALGR
//
DBGET integrated database retrieval system