ID A0A384HLQ2_9ACTN Unreviewed; 381 AA.
AC A0A384HLQ2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:PZT76321.1};
DE EC=2.5.1.48 {ECO:0000313|EMBL:PZT76321.1};
GN ORFNames=DNK56_23520 {ECO:0000313|EMBL:PZT76321.1};
OS Streptomyces sp. AC1-42W.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2218666 {ECO:0000313|EMBL:PZT76321.1, ECO:0000313|Proteomes:UP000249154};
RN [1] {ECO:0000313|EMBL:PZT76321.1, ECO:0000313|Proteomes:UP000249154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AC1-42W {ECO:0000313|EMBL:PZT76321.1,
RC ECO:0000313|Proteomes:UP000249154};
RA De Leon M.P., Montecillo A.D., Siringan M.A.T., Kim S.-G., Rosana A.R.R.;
RT "Near complete genome sequences of Streptomyces sp. strains AC1-42W
RT isolated from bat guano of Cabalyorisa Cave, Pangasinan, Philippines.";
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:PZT76321.1}.
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; QKWY01000002; PZT76321.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A384HLQ2; -.
DR Proteomes; UP000249154; Unassembled WGS sequence.
DR GO; GO:0016846; F:carbon-sulfur lyase activity; IEA:UniProt.
DR GO; GO:0003962; F:cystathionine gamma-synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0102028; F:cystathionine gamma-synthase activity (acts on O-phosphohomoserine); IEA:UniProtKB-EC.
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:UP000249154};
KW Transferase {ECO:0000313|EMBL:PZT76321.1}.
FT MOD_RES 201
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 381 AA; 40335 MW; 5CBB633D454A3B5C CRC64;
MSDQHSFETR AIHAGNTADP LTGAVVPPIY QVSTYKQDGV GGLRGGYEYS RSANPTRTAL
EENLAALEGG RRGLAFASGL AAEDCLLRTL LTPGDHVVIP NDAYGGTFRL FSKVAARWGV
EFSVADTSDV AAVRAAITPR TKAVWVETPS NPLLGITDIE AVAQVARTAG VRLVVDNTFA
SPYLQQPLAL GADVVVHSTT KYMGGHSDVV GGALITDDQD LADELVFHQN AMGAVAGPFD
AWLVLRGIKT LAVRMDRHSE NATKVAELLT RHPKVTQVLY PGLPEHRGHE IAAKQMRAFG
GMVSFRVEGG EQAAVEVCDR AKLFTLGESL GGVESLLEHP GRMTHASAAG SPLEVPADLV
RLSVGIENAD DLLADLTQAL G
//
