ID U5MNS6_CLOSA Unreviewed; 378 AA.
AC U5MNS6;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Cystathionine beta-lyase MetC {ECO:0000313|EMBL:AGX41336.1};
DE EC=4.4.1.8 {ECO:0000313|EMBL:AGX41336.1};
GN Name=metC {ECO:0000313|EMBL:AGX41336.1};
GN ORFNames=CLSA_c02840 {ECO:0000313|EMBL:AGX41336.1};
OS Clostridium saccharobutylicum DSM 13864.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1345695 {ECO:0000313|EMBL:AGX41336.1, ECO:0000313|Proteomes:UP000017118};
RN [1] {ECO:0000313|EMBL:AGX41336.1, ECO:0000313|Proteomes:UP000017118}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13864 {ECO:0000313|EMBL:AGX41336.1};
RX PubMed=24285650;
RA Poehlein A., Hartwich K., Krabben P., Ehrenreich A., Liebl W., Durre P.,
RA Gottschalk G., Daniel R.;
RT "Complete Genome Sequence of the Solvent Producer Clostridium
RT saccharobutylicum NCP262 (DSM 13864).";
RL Genome Announc. 1:e00997-13(2013).
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}.
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; CP006721; AGX41336.1; -; Genomic_DNA.
DR RefSeq; WP_022743625.1; NZ_AYXL01000184.1.
DR AlphaFoldDB; U5MNS6; -.
DR GeneID; 55472859; -.
DR KEGG; csb:CLSA_c02840; -.
DR PATRIC; fig|1345695.10.peg.1443; -.
DR eggNOG; COG0626; Bacteria.
DR HOGENOM; CLU_018986_2_0_9; -.
DR OrthoDB; 9780685at2; -.
DR Proteomes; UP000017118; Chromosome.
DR GO; GO:0004121; F:cystathionine beta-lyase activity; IEA:UniProtKB-EC.
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:SF15; CYSTATHIONINE GAMMA-LYASE; 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:AGX41336.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000017118}.
FT MOD_RES 195
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 378 AA; 41528 MW; 73256FCFF84845D9 CRC64;
MNFGTKLIHA SGDIDPATGS VSTPIYQTST FHQFDIDNFG KYDYSRSGNP TRDVLEKLIA
ELEGGERGFA FASGMAAIAS VLSIFSAGDH IIICGDVYGG TYRAATKLFS RFNIDFTFVD
ASNIEEIRSA FKENTRGLYL ETPSNPLLKV TDLRAASRIA NEHNAITIVD NTFMSPYLQR
PLELGADIVV HSATKFLGGH SDVLAGLVVT KTKELSDRVY QVQNTFGAVL GPQDSWLLIR
GIKTLKVRLD ALQKSAQKLA EWLEGRDEVE KVYYLGLESM EGRELHLEQA YGAGAVLSFK
FKDIERTTIF LNNVKNVAVA VSLGSVETIV SYPAKMSHAA IPKEEREQLG ITDTLIRVSV
GLEDIDDLLG SFQEAIEK
//
