ID A0A1I7HJB8_9GAMM Unreviewed; 391 AA.
AC A0A1I7HJB8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=cysteine-S-conjugate beta-lyase {ECO:0000256|ARBA:ARBA00012224};
DE EC=4.4.1.13 {ECO:0000256|ARBA:ARBA00012224};
GN ORFNames=SAMN04487955_104300 {ECO:0000313|EMBL:SFU60679.1};
OS Halomonas korlensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=463301 {ECO:0000313|EMBL:SFU60679.1, ECO:0000313|Proteomes:UP000198693};
RN [1] {ECO:0000313|Proteomes:UP000198693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6981 {ECO:0000313|Proteomes:UP000198693};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FPBP01000004; SFU60679.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7HJB8; -.
DR STRING; 463301.SAMN04487955_104300; -.
DR OrthoDB; 3224382at2; -.
DR Proteomes; UP000198693; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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:SFU60679.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198693}.
FT DOMAIN 30..385
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 391 AA; 42981 MW; C163800D4FAFD5AD CRC64;
MDYDFATPVE RRHPSGGRWP SQKWHRHGDD VLPLWVADMD FVSPPEVIEA LRARVDHGVF
GYGGVPDSLR ETLCDWSVEH YDWTIEPEWQ LWLPGVVPAL HLASLALTEP GDGVLTVTPI
YPPFLRVAER TGRLAQQAAM RAPDRPGDPW RLDLEALEAA ITPETRLLLW CQPHNPTGRV
WSREELAGLA SLVQHHNLLV ISDELHCDLL LDEGAHHTPL ASAFPELAAR TLTLWAPSKT
FNLAGLTTAC AVIPDDGLRR RFARMAKGLQ PDANVLGLVA AEAAYAQGDP WRRALLEVLR
GHRQRLVSRV AHWPGAAMNA PESTYLAWLD LREAVGLEGA RSPAKALLER TGVALSDGAD
FGCPGFARLN FGTTATQLEA ALDRLDGALK G
//
