ID Q0BTI4_GRABC Unreviewed; 422 AA.
AC Q0BTI4;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 24-JAN-2024, entry version 94.
DE SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:ABI61868.2};
DE EC=4.4.1.8 {ECO:0000313|EMBL:ABI61868.2};
GN OrderedLocusNames=GbCGDNIH1_0970 {ECO:0000313|EMBL:ABI61868.2};
OS Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Granulibacter.
OX NCBI_TaxID=391165 {ECO:0000313|EMBL:ABI61868.2, ECO:0000313|Proteomes:UP000001963};
RN [1] {ECO:0000313|EMBL:ABI61868.2, ECO:0000313|Proteomes:UP000001963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1260 / CGDNIH1 {ECO:0000313|Proteomes:UP000001963};
RX PubMed=17827295; DOI=10.1128/JB.00793-07;
RA Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E.,
RA Kupko J.J.III., Barbian K.D., Babar A., Dorward D.W., Holland S.M.;
RT "Genome sequence analysis of the emerging human pathogenic acetic acid
RT bacterium Granulibacter bethesdensis.";
RL J. Bacteriol. 189:8727-8736(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L,L-cystathionine = L-homocysteine + NH4(+) + pyruvate;
CC Xref=Rhea:RHEA:13965, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:58161, ChEBI:CHEBI:58199;
CC Evidence={ECO:0000256|ARBA:ARBA00001535};
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}.
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DR EMBL; CP000394; ABI61868.2; -; Genomic_DNA.
DR AlphaFoldDB; Q0BTI4; -.
DR STRING; 391165.GbCGDNIH1_0970; -.
DR KEGG; gbe:GbCGDNIH1_0970; -.
DR eggNOG; COG0626; Bacteria.
DR Proteomes; UP000001963; 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 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; IPR006233; Cys_b_lyase_bac.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR01324; cysta_beta_ly_B; 1.
DR PANTHER; PTHR43500; CYSTATHIONINE BETA-LYASE-RELATED; 1.
DR PANTHER; PTHR43500:SF1; CYSTATHIONINE BETA-LYASE-RELATED; 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:ABI61868.2};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000001963}.
FT REGION 20..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 239
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 422 AA; 46483 MW; ED41AA0E07A8260E CRC64;
MMAHGRNGAA APILRSSVMQ YNRPGPRTPS DAPNEHPDTR LVRAGRPVAK YTGVVNPPLI
RGSTVLQPDT ATRRREGKRW LEQSLTYGLN GSETHFALEN AIAEIEGGTH CQIVSSGLAA
CTVPLLGYLS AGDHLLVPDM VYGPTRDFCE GLLKQFGIET TFYTATATAH ELAPLFRPET
RVLFLESPGS HTFEVQDVAA LCALAHQHGA VTMLDNTWGI RHFQPFQHGI DLSIQALTKY
VGGHSDLLLG SITVNDEAHW RRVRSTAGML GQYASPDDCW LALRGLRTMA VRMNHQMQSA
LHIATFLSER PEIQRVLYPA LPGDPGYEMW KRDFTGAPSL FGVEFKSSFT TEQSDRFIDS
LSIFGLGASW GGYESLIMPT YGTIHRSHDI PLEGPTVRIH IGLEDPQDLI ADLTRALDAM
QR
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