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Database: UniProt
Entry: G8QUQ7_SPHPG
LinkDB: G8QUQ7_SPHPG
Original site: G8QUQ7_SPHPG 
ID   G8QUQ7_SPHPG            Unreviewed;       416 AA.
AC   G8QUQ7;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=cysteine-S-conjugate beta-lyase {ECO:0000256|ARBA:ARBA00012224};
DE            EC=4.4.1.13 {ECO:0000256|ARBA:ARBA00012224};
GN   OrderedLocusNames=SpiGrapes_2604 {ECO:0000313|EMBL:AEV30365.1};
OS   Sphaerochaeta pleomorpha (strain ATCC BAA-1885 / DSM 22778 / Grapes).
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Sphaerochaetaceae;
OC   Sphaerochaeta.
OX   NCBI_TaxID=158190 {ECO:0000313|EMBL:AEV30365.1, ECO:0000313|Proteomes:UP000005632};
RN   [1] {ECO:0000313|EMBL:AEV30365.1, ECO:0000313|Proteomes:UP000005632}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1885 / DSM 22778 / Grapes
RC   {ECO:0000313|Proteomes:UP000005632};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Munk A.C., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Ritalahtilisa K.,
RA   Loeffler F., Woyke T.;
RT   "Complete sequence of Spirochaeta sp. grapes.";
RL   Submitted (NOV-2011) 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; CP003155; AEV30365.1; -; Genomic_DNA.
DR   RefSeq; WP_014271205.1; NC_016633.1.
DR   AlphaFoldDB; G8QUQ7; -.
DR   STRING; 158190.SpiGrapes_2604; -.
DR   KEGG; sgp:SpiGrapes_2604; -.
DR   eggNOG; COG1168; Bacteria.
DR   HOGENOM; CLU_017584_15_0_12; -.
DR   OrthoDB; 367386at2; -.
DR   Proteomes; UP000005632; Chromosome.
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; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
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:UP000005632}.
FT   DOMAIN          45..403
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   416 AA;  47084 MW;  C4C57F97960EC54E CRC64;
     MQYDFDKEVN RKGSLSVKWD AHAIKSICGV SDAEPFWVAD MDFTAAPEIM DQVVQTAKSG
     VYGYPHFSGT NKLFCEWAKK RHNWEVEEKD VVICMGMLNS IALLTDILTD EKDGIIVPMP
     AYQPFVRIVN NLDRTLLRWP LSYDKEAHKF SLDWEKYEQL CKQAKLLIFC SPHNPSGLEF
     SPGELERLCR IAADNNVTII CDEIHADLSF GKHQPLLPIA QNVGCKAITC MAPSKTFNIA
     GEHYSVAIIE DEGIRKALKK RMSQLFISET SFFSTTTAMS AYRYGYDWLL QLIPYLQKNI
     AFIDGFCNEK IPQLHLIKPK ASFIALLDCS EILPLVEADA KANPDLYNSE LSPGGGLLSR
     FFGIRAKVAV NDGTWFGGED YRGFVRFNYG TQRSSIEKAF NRIEQAIAFL QTTYTR
//
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