ID W5IJ37_SCAIO Unreviewed; 403 AA.
AC W5IJ37;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=cysteine-S-conjugate beta-lyase {ECO:0000256|ARBA:ARBA00012224};
DE EC=4.4.1.13 {ECO:0000256|ARBA:ARBA00012224};
GN ORFNames=HMPREF9020_00673 {ECO:0000313|EMBL:EFG27041.1};
OS Scardovia inopinata F0304.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Scardovia.
OX NCBI_TaxID=641146 {ECO:0000313|EMBL:EFG27041.1, ECO:0000313|Proteomes:UP000005777};
RN [1] {ECO:0000313|EMBL:EFG27041.1, ECO:0000313|Proteomes:UP000005777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0304 {ECO:0000313|EMBL:EFG27041.1,
RC ECO:0000313|Proteomes:UP000005777};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Gevers D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., Chen Z., Engels R.,
RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E.R.,
RA Heiman D.I., Hepburn T.A., Howarth C., Jen D., Larson L., Mehta T.,
RA Park D., Pearson M., Richards J., Roberts A., Saif S., Shea T.D.,
RA Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., Yandava C.,
RA Izard J., Baranova O.V., Blanton J.M., Tanner A.C., Dewhirst F., Haas B.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Scardovia inopinata F0304.";
RL Submitted (JAN-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:EFG27041.1}.
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DR EMBL; ADCX01000003; EFG27041.1; -; Genomic_DNA.
DR RefSeq; WP_006293040.1; NZ_GG770225.1.
DR AlphaFoldDB; W5IJ37; -.
DR eggNOG; COG1168; Bacteria.
DR HOGENOM; CLU_017584_15_0_11; -.
DR Proteomes; UP000005777; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000005777}.
FT DOMAIN 49..390
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 403 AA; 44726 MW; DCFDAD19DA545452 CRC64;
MTDTISHASE ACDHDSSSRP FPFEAVDRSQ IDSVKWSTKP HELPMWVADM DFATAPAIVD
AVRERVSNPT YGYSLVPDEF GQTIAAWWRQ EYQTQINPAD VIFAAGVIPA ISSAIRSLTN
PGEKIVVQSP VYNNFYTSII NNGRQVCDAP LIYQAGEYSM DFAALEEAFS DPLTTMMILC
NPQNPTGNIW SADDLAIIAQ LAKDHHVIVV SDEIHCDIRR PGLAHTPFAS VYPAAREVAV
TCNSPSKAFN IAGLHSAYLV VSTDWIRRRV QAQLIRDGVA EPTVFSCPAA IAAYAHSRDW
LRAVNHYIQE NKDYARTKLS KNLPNLHIPR SDATYLLWLD CRAFTSDADL LSRQIREQTG
LYLSSGKMYG PSGAAFLRMN LGTSRTLVED GTDRLIQALS RQQ
//