ID R7IB67_9FIRM Unreviewed; 396 AA.
AC R7IB67;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=cysteine-S-conjugate beta-lyase {ECO:0000256|ARBA:ARBA00012224};
DE EC=4.4.1.13 {ECO:0000256|ARBA:ARBA00012224};
GN ORFNames=BN770_01829 {ECO:0000313|EMBL:CDE48810.1};
OS Faecalibacterium sp. CAG:74.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Faecalibacterium.
OX NCBI_TaxID=1262897 {ECO:0000313|EMBL:CDE48810.1, ECO:0000313|Proteomes:UP000018328};
RN [1] {ECO:0000313|EMBL:CDE48810.1, ECO:0000313|Proteomes:UP000018328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:74 {ECO:0000313|Proteomes:UP000018328};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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}.
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:CDE48810.1}.
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DR EMBL; CBJB010000120; CDE48810.1; -; Genomic_DNA.
DR AlphaFoldDB; R7IB67; -.
DR Proteomes; UP000018328; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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 Aminotransferase {ECO:0000313|EMBL:CDE48810.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018328};
KW Transferase {ECO:0000313|EMBL:CDE48810.1}.
FT DOMAIN 34..380
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 396 AA; 44301 MW; C631CAE5FFB2DF05 CRC64;
MHTFDESYFD AGLDRRGTRC EKWDGTEKES VLPLWVADMD FPSPPEVAEA IAVRALHPTY
GYTLVLPDDT RALTGFWQRR HNLTIQDEWV MMIPCVVTGI RLALLALTKP GDGVMIQSPV
YGPFRFSVEA TERRLMDAPL KRDDTGRYSM DLDAVEKQLQ AGAKALVLCN PHNPVSRAWK
REELQALIDL LARYGAYLIA DEIHADFVYA PEQFVPVLSL AQKNVLSLCA ASKTFNLAGL
EQAAMLVPDE AVRAKINTEM ERAGVRSGNL FALEGTRAAY EYGDAWLDGL MHYLDGNRKH
LTALVKQELP QAVLTPMEAT YLGWLDLRAY GMNCEELMAR TLKHGVQFTE GTFFGEGGEG
FLRVNIGCPR RNIIEGIHRL KEALDEAVEE KAHGVD
//
