ID A0A1C3CSY7_9GAMM Unreviewed; 400 AA.
AC A0A1C3CSY7;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:ODA11843.1};
GN ORFNames=BBP83_13700 {ECO:0000313|EMBL:ODA11843.1};
OS Acinetobacter celticus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1891224 {ECO:0000313|EMBL:ODA11843.1, ECO:0000313|Proteomes:UP000186553};
RN [1] {ECO:0000313|EMBL:ODA11843.1, ECO:0000313|Proteomes:UP000186553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANC 4603 {ECO:0000313|EMBL:ODA11843.1,
RC ECO:0000313|Proteomes:UP000186553};
RA Radolfova-Krizova L., Nemec A.;
RT "Acinetobacter sp. ANC 4603.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:ODA11843.1}.
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DR EMBL; MBDL01000015; ODA11843.1; -; Genomic_DNA.
DR RefSeq; WP_068889867.1; NZ_MBDL01000015.1.
DR AlphaFoldDB; A0A1C3CSY7; -.
DR STRING; 1891224.BBP83_13700; -.
DR OrthoDB; 9805807at2; -.
DR Proteomes; UP000186553; Unassembled WGS sequence.
DR GO; GO:0004121; F:cystathionine beta-lyase activity; IEA:InterPro.
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 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.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2}.
FT MOD_RES 209
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 400 AA; 44920 MW; 5D6FE6A83FE8B028 CRC64;
MKKNPQTALI HAPRKAPQYV STIQPPLFRA STIIFDNTNA LFNRHWTDRY DYSYGTHGTP
TTFTLADNIA QLEGGEFCLL APSGLSAINL VNSCFLSQGD EVWVADNIYG PNMEHLRNLE
MRYGITVKVY NPIDVASFQP TEKAKLIWLE AAGSVTLEFP DLNNLVKKAK AHHVLSALDN
TWGAGLAFNA FDFGDEHLSV DLTAHALTKY PSGGGDILMG SVVTRDEKLH QQLFRMHALQ
GISISGDDTA QVQRSLASMQ IRYQHQSEST LTLLAWLKQQ TEFAQILHPA DETSAGHTYW
KEICSTEQSA GLVSVIFKPE YHLKDVRHFC DALSLFKLGF SWGGPISLVM LYNLKEMRTL
EHTHLQQGLL VRFCIGLEHP QDLIQDIKNA LKQLKRQQLE
//
