ID D1Y572_9BACT Unreviewed; 393 AA.
AC D1Y572;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=cysteine-S-conjugate beta-lyase {ECO:0000256|ARBA:ARBA00012224};
DE EC=4.4.1.13 {ECO:0000256|ARBA:ARBA00012224};
GN Name=patB {ECO:0000313|EMBL:EFB90527.1};
GN ORFNames=HMPREF7215_1858 {ECO:0000313|EMBL:EFB90527.1};
OS Pyramidobacter piscolens W5455.
OC Bacteria; Synergistota; Synergistia; Synergistales;
OC Dethiosulfovibrionaceae; Pyramidobacter.
OX NCBI_TaxID=352165 {ECO:0000313|EMBL:EFB90527.1, ECO:0000313|Proteomes:UP000006462};
RN [1] {ECO:0000313|EMBL:EFB90527.1, ECO:0000313|Proteomes:UP000006462}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W5455 {ECO:0000313|EMBL:EFB90527.1,
RC ECO:0000313|Proteomes:UP000006462};
RA Shrivastava S., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RL Submitted (DEC-2009) 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:EFB90527.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ADFP01000075; EFB90527.1; -; Genomic_DNA.
DR RefSeq; WP_009165003.1; NZ_ADFP01000075.1.
DR AlphaFoldDB; D1Y572; -.
DR STRING; 352165.HMPREF7215_1858; -.
DR eggNOG; COG1168; Bacteria.
DR OrthoDB; 9802872at2; -.
DR Proteomes; UP000006462; Unassembled WGS sequence.
DR GO; GO:0004121; F:cystathionine beta-lyase activity; IEA:UniProtKB-EC.
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:EFB90527.1}.
FT DOMAIN 58..382
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 393 AA; 44949 MW; F3476B671A873834 CRC64;
MKYDFDKVIE RRGTQSSKWD NVGPRVGNPD ALPMWVADTD FQAPQPVVDA VVKRAQHPIY
GYTFVVPEFQ KVTVDWVKRR HGWEIQPEWL VFAAGVVPVM NTMAQIYSEP GDEIVIQQPV
YPQFANAVRD TGRVISDNGL LYKNGRYEID FDDLERRASS PKAKLMFFCN PHNPAGRVWT
VEELKKVAEI CLKHHIILVS DEIHSDLILF GHKHTPLASL DKRYGEMTVT CYAPSKTFNT
AGLRGSGIVV PNPEIRAKLE KQFKRNRAIQ QNIFALPAYI VAYTECDDYL EQLLAYLEGN
VLYIEEFLKE KMPKIRMVHP EATYLAWLDC SGTGMEGDAL ADFFINRCKV AINRGDSFGP
ECKKFVRLNF GCPRITLEKG LGQIYAEYQR LFR
//
