ID A6BMK1_STRCV Unreviewed; 388 AA.
AC A6BMK1;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=cysteine-S-conjugate beta-lyase {ECO:0000256|ARBA:ARBA00012224};
DE EC=4.4.1.13 {ECO:0000256|ARBA:ARBA00012224};
GN Name=lcd {ECO:0000313|EMBL:BAF64501.1};
OS Streptococcus constellatus.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus; Streptococcus anginosus group.
OX NCBI_TaxID=76860 {ECO:0000313|EMBL:BAF64501.1};
RN [1] {ECO:0000313|EMBL:BAF64501.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IMU108 {ECO:0000313|EMBL:BAF64501.1};
RX PubMed=18402612; DOI=10.1111/j.1399-302X.2007.00419.x;
RA Yoshida Y., Ito S., Sasaki T., Kishi M., Kurota M., Suwabe A.,
RA Kunimatsu K., Kato H.;
RT "Molecular and enzymatic characterization of betaC-S lyase in Streptococcus
RT constellatus.";
RL Oral Microbiol. Immunol. 23:245-253(2008).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. MalY/PatB cystathionine beta-lyase subfamily.
CC {ECO:0000256|ARBA:ARBA00037974}.
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DR EMBL; AB327003; BAF64501.1; -; Genomic_DNA.
DR AlphaFoldDB; A6BMK1; -.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd00609; AAT_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; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR027619; C-S_lyase_PatB-like.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR04350; C_S_lyase_PatB; 1.
DR PANTHER; PTHR43525; PROTEIN MALY; 1.
DR PANTHER; PTHR43525:SF1; PROTEIN MALY; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:BAF64501.1}.
FT DOMAIN 37..382
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 388 AA; 44396 MW; 83B80E2C88D72534 CRC64;
MSKYNFQTAP NRLSHHTYKW KETETDPQLL PAWIADMDFE VMPEVKNAIH DYAEQLVYGY
TYASDELLQA VLDWEKSEHQ YSFDKDSIVF VEGVVPAISI AIQAFTKEGE AVLINSPVYP
PFARSVQLNH RKLVSNSLKE EHGLFQIDFE QLEKDIVEND VKLYLLCNPH NPGGRVWEKE
VLERVGQLCQ KHHVILVSDE IHQDLTLFGH QHISFNTVSP DFKDFALVLS SATKTFNIAG
TKNSYAIIEN PTLCAQFKHQ QLVNNHHEVS SLGYIATETA YRYGKPWLVA LKAVLEENIQ
FAVEYFAKEA PRLKVMKPQG TYLIWLDFSD YGLTDDELFA LLHDQAKVIL NRGSDYGSEG
ELHARLNIAT PKSLVKEICK RIVRCLPK
//