ID A0A0R1XCB1_9LACO Unreviewed; 403 AA.
AC A0A0R1XCB1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=cysteine-S-conjugate beta-lyase {ECO:0000256|ARBA:ARBA00012224};
DE EC=4.4.1.13 {ECO:0000256|ARBA:ARBA00012224};
GN ORFNames=FC91_GL002550 {ECO:0000313|EMBL:KRM27341.1};
OS Schleiferilactobacillus harbinensis DSM 16991.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Schleiferilactobacillus.
OX NCBI_TaxID=1122147 {ECO:0000313|EMBL:KRM27341.1, ECO:0000313|Proteomes:UP000050949};
RN [1] {ECO:0000313|EMBL:KRM27341.1, ECO:0000313|Proteomes:UP000050949}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16991 {ECO:0000313|EMBL:KRM27341.1,
RC ECO:0000313|Proteomes:UP000050949};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRM27341.1}.
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DR EMBL; AZFW01000050; KRM27341.1; -; Genomic_DNA.
DR RefSeq; WP_035439821.1; NZ_AZFW01000050.1.
DR AlphaFoldDB; A0A0R1XCB1; -.
DR PATRIC; fig|1122147.4.peg.2631; -.
DR eggNOG; COG1168; Bacteria.
DR OrthoDB; 9802872at2; -.
DR Proteomes; UP000050949; 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:KRM27341.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000050949};
KW Transferase {ECO:0000313|EMBL:KRM27341.1}.
FT DOMAIN 56..392
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 403 AA; 45660 MW; EF1CC2306DDDAC4D CRC64;
MAIELTPENK AFIKTHLVDR HHTNTLKWDA LDDRFGNPDL LPLWVADMEF KTAQPVRDAL
VKRVEEGVFG YSYIPDSYKA AFIDWQRDRH GITVKPEWLR FDTGVVNSLY GLVNWLTEPG
DPVLIFQPVY YPFANAVTDT HRKLISCNLL DTPQGWQVDY EALHKIITED KPKLVIWCSP
HNPVGRIWKP EELETILTPL VANGIPVISD EIHEDFEIGE QPFTSVLDVA DGRFRDGVIV
VNAPSKTFNL ATLLHSHVII PNAAWRKDYD SFIKSIHQTE PSLLGVVAGE AAYRYGAAWL
DQILQIIRYN DGQVREILRQ APGVKLHPLE GTYLLYVDLG QYIPADKIRD FVQNHCHLAV
DYGAWFSPQT PTFIRLNLAT DPAIVARAAN QIVTALQETV PAL
//
