ID I8TXI8_9FIRM Unreviewed; 380 AA.
AC I8TXI8;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Cystathionine gamma-lyase {ECO:0000313|EMBL:AJQ28273.1};
DE EC=4.4.1.1 {ECO:0000313|EMBL:AJQ28273.1};
GN ORFNames=JBW_02930 {ECO:0000313|EMBL:AJQ28273.1};
OS Pelosinus fermentans JBW45.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Pelosinus.
OX NCBI_TaxID=1192197 {ECO:0000313|EMBL:AJQ28273.1, ECO:0000313|Proteomes:UP000005361};
RN [1] {ECO:0000313|EMBL:AJQ28273.1, ECO:0000313|Proteomes:UP000005361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBW45 {ECO:0000313|EMBL:AJQ28273.1,
RC ECO:0000313|Proteomes:UP000005361};
RX PubMed=26404608;
RA De Leon K.B., Utturkar S.M., Camilleri L.B., Elias D.A., Arkin A.P.,
RA Fields M.W., Brown S.D., Wall J.D.;
RT "Complete Genome Sequence of Pelosinus fermentans JBW45, a Member of a
RT Remarkably Competitive Group of Negativicutes in the Firmicutes Phylum.";
RL Genome Announc. 3:e01090-e01015(2015).
RN [2] {ECO:0000313|Proteomes:UP000005361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBW45 {ECO:0000313|Proteomes:UP000005361};
RA De Leon K.B., Utturkar S.M., Camilleri L.B., Arkin A.P., Fields M.W.,
RA Brown S.D., Wall J.D.;
RT "Complete Genome Sequence of Pelosinus fermentans JBW45.";
RL Submitted (FEB-2015) 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|RuleBase:RU362118}.
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DR EMBL; CP010978; AJQ28273.1; -; Genomic_DNA.
DR RefSeq; WP_007957691.1; NZ_CP010978.1.
DR AlphaFoldDB; I8TXI8; -.
DR STRING; 1192197.JBW_02930; -.
DR KEGG; pft:JBW_02930; -.
DR HOGENOM; CLU_018986_2_0_9; -.
DR OrthoDB; 9780685at2; -.
DR Proteomes; UP000005361; Chromosome.
DR GO; GO:0004123; F:cystathionine gamma-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0080146; F:L-cysteine desulfhydrase activity; IEA:UniProtKB-EC.
DR GO; GO:0044540; F:L-cystine L-cysteine-lyase (deaminating); 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:AJQ28273.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000005361}.
FT MOD_RES 197
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 380 AA; 40909 MW; E214B359F2816F1B CRC64;
MKEKDFATKL LHVGVEIDAH TGAVSTPIYQ VSTFHQNIDQ PQEYEYSRSG NPTRKALETT
IAELEEGIAG FAFASGIAAV STALLLFQQG DHILAPKDVY GGTYRLLSKV CGKWGIDHTF
VDTTDLKEIE KAVKSNTKAI VLESPSNPLL KVSDLPQICA WAKSKGIITI VDNTFMTPYL
QRPLTFGADI VVHSATKFLA GHSDVVAGLI ATNSKKLADE LYFLQNALGA VLGPQDCWLT
MRGIKTLKVR MDHSQQAALK IAKALAEHPN VKAVHYPGLS EDPGYELLKG QAAGFGAVLS
FEVESAALAK RIMRNVKLSA VAVSLGSVES ILSYPVSMSH AAIEPHVRQA LGISDGLLRL
SVGLEDANDL LADLTSAMEE
//
