ID A0A2M6VH89_9BURK Unreviewed; 410 AA.
AC A0A2M6VH89;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:PIT77780.1};
GN ORFNames=B9Z42_04860 {ECO:0000313|EMBL:PIT77780.1};
OS Limnohabitans sp. B9-3.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Limnohabitans.
OX NCBI_TaxID=1100707 {ECO:0000313|EMBL:PIT77780.1, ECO:0000313|Proteomes:UP000228506};
RN [1] {ECO:0000313|EMBL:PIT77780.1, ECO:0000313|Proteomes:UP000228506}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B9-3 {ECO:0000313|EMBL:PIT77780.1,
RC ECO:0000313|Proteomes:UP000228506};
RA Kasalicky V., Mehrshad M., Andrei S.-A., Salcher M., Kratochvilova H.,
RA Simek K., Ghai R.;
RT "Unexpected and diverse lifestyles within the genus Limnohabitans.";
RL Submitted (APR-2017) 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:PIT77780.1}.
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DR EMBL; NESI01000002; PIT77780.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M6VH89; -.
DR OrthoDB; 9805807at2; -.
DR Proteomes; UP000228506; 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 Lyase {ECO:0000313|EMBL:PIT77780.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000228506}.
FT MOD_RES 216
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 410 AA; 44118 MW; 007301C979370829 CRC64;
MTRSTHLIHH AYQPPAEFEA PQVGVFKAST VIFPNVAAMR TREWMDKSAY TYGLHGTPTT
FTLEERLATL EGGTHCILTP SGLAAIAHVD FALLKTGDEV LIPDNAYAPN KSLAEGELAH
FGITHQVYDP LDVNDLAARI TPRTRLVWLE APGSVTMEFP DLVALVQLCK SRGVLCALDN
TWGAGLAFNA FDLTPGQGAQ GQPPLGVDLT IHALTKYPSG GGDVLMGSIV TRSDELAQVL
KLSHMRLGTG VGANDAEMVL RSLSSMPLRY KAQDAAARTL AAWCTSQPAF SQVLHPALSS
SPGHAQWQQL CVTPHEPEGL AAGIYSVVMD ERFTSAQVDA FCDALQLFKI GYSWGGPMSL
VMPYNMASSR ARATAHMQRG RVVRFCIGLE AASHLQADIL QALQTANLQA
//
