ID A0A329LUN6_9BACL Unreviewed; 378 AA.
AC A0A329LUN6;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Cystathionine beta-lyase/cystathionine gamma-synthase {ECO:0000313|EMBL:RAV11148.1};
GN ORFNames=DQG23_36800 {ECO:0000313|EMBL:RAV11148.1};
OS Paenibacillus contaminans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=450362 {ECO:0000313|EMBL:RAV11148.1, ECO:0000313|Proteomes:UP000250369};
RN [1] {ECO:0000313|EMBL:RAV11148.1, ECO:0000313|Proteomes:UP000250369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CKOBP-6 {ECO:0000313|EMBL:RAV11148.1,
RC ECO:0000313|Proteomes:UP000250369};
RX PubMed=19126735; DOI=10.1099/ijs.0.001495-0;
RA Chou J.H., Lee J.H., Lin M.C., Chang P.S., Arun A.B., Young C.C.,
RA Chen W.M.;
RT "Paenibacillus contaminans sp. nov., isolated from a contaminated
RT laboratory plate.";
RL Int. J. Syst. Evol. Microbiol. 59:125-129(2009).
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 -!- 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:RAV11148.1}.
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; QMFB01000039; RAV11148.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A329LUN6; -.
DR OrthoDB; 9780685at2; -.
DR Proteomes; UP000250369; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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:SF90; 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.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:RAV11148.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000250369}.
FT MOD_RES 195
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 378 AA; 41711 MW; 94F799868D09782B CRC64;
MKSKEDIIAH LGDEYDRYLG AIVPPIFQNS LFTRKTVNHG YTYTRVANPT TEIAEMKIAA
LEGGEAARCF SSGMAAITAA LAHYLEKDSH VICPRAVYTP TKGFLETYMK KFGCEVTLVS
GDSVEEFEQA IRPNTKVIYL ESPLSNIFTL QDLEAISALA NSRGIATIID NTWATPLYQN
PLEYGIDLVV HSASKYLGGH SDILGGVVVG SKETLEAITH NERSMFGAVM DPHQSWLLIR
SLRTLPVRMK QHQENGLKVA SFLEQHPLVS AVCHPGLTSH PQYELGRKQM TGYSGLLSFV
PKGDKQQIMK MMKSLRYFEE GPSWGGFESL INSPGLWVNE ETSVLAGIPV GLLRISVGLE
SADSIIDDLD RALNEMTR
//
