ID A0A085AB64_9ENTR Unreviewed; 396 AA.
AC A0A085AB64;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:KFC07459.1};
DE EC=4.4.1.8 {ECO:0000313|EMBL:KFC07459.1};
GN ORFNames=GTGU_01843 {ECO:0000313|EMBL:KFC07459.1};
OS Trabulsiella guamensis ATCC 49490.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Trabulsiella.
OX NCBI_TaxID=1005994 {ECO:0000313|EMBL:KFC07459.1, ECO:0000313|Proteomes:UP000028630};
RN [1] {ECO:0000313|EMBL:KFC07459.1, ECO:0000313|Proteomes:UP000028630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49490 {ECO:0000313|EMBL:KFC07459.1,
RC ECO:0000313|Proteomes:UP000028630};
RA Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of
RT the evolutionary history of the Enterobacteriaceae.";
RL Submitted (MAY-2014) 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:KFC07459.1}.
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DR EMBL; JMTB01000062; KFC07459.1; -; Genomic_DNA.
DR RefSeq; WP_038155928.1; NZ_JMTB01000062.1.
DR AlphaFoldDB; A0A085AB64; -.
DR eggNOG; COG0626; Bacteria.
DR OrthoDB; 9805807at2; -.
DR Proteomes; UP000028630; Unassembled WGS sequence.
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.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:KFC07459.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2}.
FT MOD_RES 211
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 396 AA; 43563 MW; D427F6EE09C57090 CRC64;
MKDSIRLETQ LVIAGRDKRY TQGAVNPVIQ RASSLVFNSV KEKKFATANR ANGELFYGRR
GTYTHFAFQK AMSELEGGVG CALYPCGAAA VANAILAFVE SGDHILVTGA AYEPTQDFCT
KILSKFNVET TYYDPMIGAG IADLIRPNTR VVFLESPSSI TMEVQDVPGM VKAIRSVNPE
IVIMIDNTWA AGVLFKALDF GVDISIQAGT KYTIGHSDGM LGTAVSNARC WDRLRENSYL
MGQTLDADTA YNGSRGLRTL AIRLRQHEES SIKIARWLMN RPEVARVNHP ALAQCPGHEY
FQRDFSGSSG LFSFVLKKRL SDEQLAHFLD NFTLFHMAYS WGGFESLILA NQPEELNEIR
PAGAVDFTGT LVRVHIGLEA VEDLIADLDA GFGRIA
//
