ID F7ZLZ6_ROSLO Unreviewed; 390 AA.
AC F7ZLZ6;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
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:AEI95390.1};
GN OrderedLocusNames=RLO149_c034490 {ECO:0000313|EMBL:AEI95390.1};
OS Roseobacter litoralis (strain ATCC 49566 / DSM 6996 / JCM 21268 / NBRC
OS 15278 / OCh 149).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseobacter.
OX NCBI_TaxID=391595 {ECO:0000313|EMBL:AEI95390.1, ECO:0000313|Proteomes:UP000001353};
RN [1] {ECO:0000313|EMBL:AEI95390.1, ECO:0000313|Proteomes:UP000001353}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49566 / DSM 6996 / JCM 21268 / NBRC 15278 / OCh 149
RC {ECO:0000313|Proteomes:UP000001353};
RX PubMed=21693016; DOI=10.1186/1471-2164-12-324;
RA Kalhoefer D., Thole S., Voget S., Lehmann R., Liesegang H., Wollher A.,
RA Daniel R., Simon M., Brinkhoff T.;
RT "Comparative genome analysis and genome-guided physiological analysis of
RT Roseobacter litoralis.";
RL BMC Genomics 12:324-324(2011).
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}.
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DR EMBL; CP002623; AEI95390.1; -; Genomic_DNA.
DR RefSeq; WP_013963285.1; NC_015730.1.
DR AlphaFoldDB; F7ZLZ6; -.
DR STRING; 391595.RLO149_c034490; -.
DR KEGG; rli:RLO149_c034490; -.
DR eggNOG; COG1168; Bacteria.
DR HOGENOM; CLU_017584_15_0_5; -.
DR OrthoDB; 3224382at2; -.
DR Proteomes; UP000001353; Chromosome.
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:AEI95390.1}.
FT DOMAIN 39..382
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 390 AA; 43775 MW; 402A5FED60DC3133 CRC64;
MSFNDPIERR GTHSSKWDMM EKLYDVPQQD GIAMWTADSD YATAPCVIDA LRRAADHGVF
GYMPIHDDYL NAIQWWMKTR HNWDIDTSWA LTSQGLGNAI ALCLDLWTDP GARVVIFTPV
YHEFQIKIEK AGREAVTCPL KHTGDSYVLD LEDAQSRLDG SEQMLIWCSP QNPSGRVWTT
DELRGIAEFA ARNDLILVSD EIHHDLVFPD HTFVPMHIAA PEVEDRLIVL TAASKTFNIA
GQRTGNMIIP DAKLRKEMQH RLNTLDYKPA ALSLQMITAA YSPEGAKWAD AQIRHLDQNR
KTFDAAIATI PGVTSMPLQA TYLAWVDFSG TGMSYDEISQ RVRKSARIAP SAGPDFGPGG
ETFLRFNLAT QHHRVEEACA RLKDAFSDLQ
//
