ID A0A0C1UJ67_9ACTN Unreviewed; 386 AA.
AC A0A0C1UJ67;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:KIE51808.1};
GN ORFNames=MB52_01445 {ECO:0000313|EMBL:KIE51808.1};
OS marine actinobacterium MedAcidi-G1.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1550399 {ECO:0000313|EMBL:KIE51808.1, ECO:0000313|Proteomes:UP000031399};
RN [1] {ECO:0000313|EMBL:KIE51808.1, ECO:0000313|Proteomes:UP000031399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mizuno C.M., Rodriguez-Valera F., Ghai R.;
RT "Novel reconstructed genomes of marine planktonic Acidimicrobiales.";
RL Submitted (SEP-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:KIE51808.1}.
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; JUEM01000003; KIE51808.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C1UJ67; -.
DR Proteomes; UP000031399; 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.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2}.
FT MOD_RES 205
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 386 AA; 41565 MW; 3714D78CC40AF609 CRC64;
MSGFEDHEDF GFETRAIRAG QPHDSRTGGV VTPIALSTTF AQDAVGQPKF GYEYARTGNP
TRHAYETCLA SLECAQHGFA FSSGMAAEDS LLRFLQPGDK IILGNDAYGG SFRLIDKIYG
RNKISNEAID LSDPNSIKEA WTSETKIVWL ETPTNPLLNV VDIQKISNIT HELGGLLIVD
NTFATPYLQK PISLGADAVV HSATKYLGGH SDVVGGFVAT NDEKLVEHLS FIQNAVGAVP
SPFDCYLVLR GIKTLAVRMD RHCENAKAIV SLLSEHPKVK QVFYPGLESN KGHEIAKNQM
TNFGGMVSFT VSGGLAMAEK VSASTKVFTL AESLGAVESL IEHPGIMTHA SVAGSALEVP
EDLIRISVGI ESIEDLVEDL EQALSI
//