ID J2XL75_9PSED Unreviewed; 392 AA.
AC J2XL75;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Cystathionine beta-lyase/cystathionine gamma-synthase {ECO:0000313|EMBL:EJN25420.1};
GN ORFNames=PMI35_04038 {ECO:0000313|EMBL:EJN25420.1};
OS Pseudomonas sp. GM78.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1144337 {ECO:0000313|EMBL:EJN25420.1, ECO:0000313|Proteomes:UP000007302};
RN [1] {ECO:0000313|EMBL:EJN25420.1, ECO:0000313|Proteomes:UP000007302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM78 {ECO:0000313|EMBL:EJN25420.1,
RC ECO:0000313|Proteomes:UP000007302};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:EJN25420.1}.
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DR EMBL; AKJF01000116; EJN25420.1; -; Genomic_DNA.
DR RefSeq; WP_008061126.1; NZ_AKJF01000116.1.
DR AlphaFoldDB; J2XL75; -.
DR PATRIC; fig|1144337.3.peg.3901; -.
DR OrthoDB; 9805807at2; -.
DR Proteomes; UP000007302; 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 Lyase {ECO:0000313|EMBL:EJN25420.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2}.
FT MOD_RES 206
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 392 AA; 42608 MW; 0F59F828EC17AAA3 CRC64;
MSQHDENAPP RGFATRVIHA GQTPDPSTGA LMPPIYANST YLQQSPGVHK GLDYGRSHNP
TRWALERCVA DLEGGTRGFA FASGLATIST VLELVDAGSH IVSGNDLYGG TFRLFDKVRQ
RSAGHRFSFV DLTDLAAFKA ALQDDTRMVM VETPSNPLLR LTDLAAIART CRDRGIICVA
DNTFASPWIQ RPLELGFDIV LHSTTKYLNG HSDVIGGIAV VGQNAELAER LGFLQNAVGA
IAGPFDAFLT LRGVKTLALR MERHCSNALE LAQWLERQPQ VARVYYPGLP SHPQHELARQ
QMRGYGGMIS VDLNTDLAGS RRFLENVRIF ALAESLGGVE SLIEHPAIMT HATIPVETRA
QLGIGDALVR LSVGVEDIED LRADLAQALA RI
//
