ID Q2S3E4_SALRD Unreviewed; 408 AA.
AC Q2S3E4;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE SubName: Full=Cystathionine beta-lyase MetC {ECO:0000313|EMBL:ABC46359.1};
GN OrderedLocusNames=SRU_1161 {ECO:0000313|EMBL:ABC46359.1};
OS Salinibacter ruber (strain DSM 13855 / M31).
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salinibacteraceae;
OC Salinibacter.
OX NCBI_TaxID=309807 {ECO:0000313|EMBL:ABC46359.1, ECO:0000313|Proteomes:UP000008674};
RN [1] {ECO:0000313|EMBL:ABC46359.1, ECO:0000313|Proteomes:UP000008674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13855 / CECT 5946 / M31
RC {ECO:0000313|Proteomes:UP000008674};
RX PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA Mongodin E.F., Nelson K.E., Daugherty S., Deboy R.T., Wister J., Khouri H.,
RA Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K.,
RA Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L.,
RA Legault B., Rodriguez-Valera F.;
RT "The genome of Salinibacter ruber: convergence and gene exchange among
RT hyperhalophilic bacteria and archaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005).
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|RuleBase:RU362118}.
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DR EMBL; CP000159; ABC46359.1; -; Genomic_DNA.
DR RefSeq; WP_011403915.1; NC_007677.1.
DR RefSeq; YP_445287.1; NC_007677.1.
DR AlphaFoldDB; Q2S3E4; -.
DR STRING; 309807.SRU_1161; -.
DR EnsemblBacteria; ABC46359; ABC46359; SRU_1161.
DR GeneID; 83728068; -.
DR KEGG; sru:SRU_1161; -.
DR eggNOG; COG0626; Bacteria.
DR HOGENOM; CLU_018986_2_0_10; -.
DR OrthoDB; 9803729at2; -.
DR Proteomes; UP000008674; Chromosome.
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:SF75; 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:UP000008674}.
FT REGION 386..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 197
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 408 AA; 43294 MW; 52203C9257BC4218 CRC64;
MDLDPETTLS LAGQDLDDTF NSVVPPLYQS AIFQFEDVGE TKGYDYTRSG NPTRAALEDT
LADLDGGAGA VACATGMAAV STVTSLFDAG AHLICAHDCY GGTERLFSCL DDQDKLSVSY
EDLSDRDALA DAVRPETTAL WVETPSNPLL RIVDLEALSE FADAHDLLLV VDNTFLSPLL
QRPIDYGADL VVYSTTKYLN GHSDVVGGAI IARTEALADR VDFAANAHGT VAAPFDSWLV
LRGAKTLPVR LRQHETNARA LARSLDEHPA VQRVCYPGLY DHPGHEIARA QQNGYGGMVS
FFVDDEQVDV EALLRSTEVF ALAESLGGVE SLIEHPATMS HASMAPEQRE AAGITNGLIR
LSVGIESTDD LRADLSQALT AAGAEAAASG HDTPVSAEAQ APASEGTC
//
