ID R5FE56_9BACT Unreviewed; 398 AA.
AC R5FE56;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=cysteine-S-conjugate beta-lyase {ECO:0000256|ARBA:ARBA00012224};
DE EC=4.4.1.13 {ECO:0000256|ARBA:ARBA00012224};
GN ORFNames=BN812_00669 {ECO:0000313|EMBL:CCY03153.1};
OS Prevotella sp. CAG:924.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1262938 {ECO:0000313|EMBL:CCY03153.1, ECO:0000313|Proteomes:UP000018357};
RN [1] {ECO:0000313|EMBL:CCY03153.1, ECO:0000313|Proteomes:UP000018357}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:924 {ECO:0000313|Proteomes:UP000018357};
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:CCY03153.1}.
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DR EMBL; CAXK010000192; CCY03153.1; -; Genomic_DNA.
DR AlphaFoldDB; R5FE56; -.
DR STRING; 1262938.BN812_00669; -.
DR Proteomes; UP000018357; 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:UP000018357}.
FT DOMAIN 25..377
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 398 AA; 45222 MW; D2F97D9C7D3E9142 CRC64;
MAFNFEQTVN RRGTGSYKWD SVPEDVLPLW VADMDYPVAP AIQKAVQARA AHPVFGYTKV
MDSYYDAIIS WYHRRHGWDI DRKWILYTQS VVPALSCTLK ALTLPGEKVM TFTPAYNCFF
SSIANQGCQL DEVPLVRESD SYVIDFDLLE EHCSDEKATV LLLCNPHNPT GRVWTPAELE
KIGEICERHH VIVVSDEIHC EIIMPGYTFT PFAAVNERNQ SIAVTLQSPS KSFNTAGLQI
ANIITSQDGW RRRIDRMINV YEVCDVNPFG PVALEAAYNE SEDWLKELNE HIASNYQYLK
DFFREELPMA EVIRMEGTYL AWIDIMAFEL TSDEAADACL RDGKVKICSG TLYGRRTGQG
YLRINLACPR ETLKQGLIRV ARVLSQYCDE PENEGCPA
//
