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Database: UniProt
Entry: A0A327M2B8_9RHOB
LinkDB: A0A327M2B8_9RHOB
Original site: A0A327M2B8_9RHOB 
ID   A0A327M2B8_9RHOB        Unreviewed;       348 AA.
AC   A0A327M2B8;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Cystathionine gamma-lyase {ECO:0000313|EMBL:RAI56706.1};
DE            EC=4.4.1.1 {ECO:0000313|EMBL:RAI56706.1};
GN   ORFNames=DOO74_02305 {ECO:0000313|EMBL:RAI56706.1};
OS   Rhodobacteraceae bacterium AsT-22.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=2230886 {ECO:0000313|EMBL:RAI56706.1, ECO:0000313|Proteomes:UP000249713};
RN   [1] {ECO:0000313|EMBL:RAI56706.1, ECO:0000313|Proteomes:UP000249713}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AsT-22 {ECO:0000313|EMBL:RAI56706.1,
RC   ECO:0000313|Proteomes:UP000249713};
RA   Zhirakovskaya E.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU362118};
CC   -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC       {ECO:0000256|RuleBase:RU362118}.
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:RAI56706.1}.
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DR   EMBL; QLIW01000001; RAI56706.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A327M2B8; -.
DR   OrthoDB; 9805807at2; -.
DR   Proteomes; UP000249713; Unassembled WGS sequence.
DR   GO; GO:0004123; F:cystathionine gamma-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0080146; F:L-cysteine desulfhydrase activity; IEA:UniProtKB-EC.
DR   GO; GO:0044540; F:L-cystine L-cysteine-lyase (deaminating); IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019346; P:transsulfuration; IEA:InterPro.
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; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11808:SF93; CYSTATHIONINE GAMMA-LYASE-RELATED; 1.
DR   PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 1.
DR   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   PIRSF; PIRSF001434; CGS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:RAI56706.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000249713}.
FT   MOD_RES         185
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   348 AA;  36511 MW;  2666D11E5EA35FFC CRC64;
     MLHARSGALE PGDPVPEPLV MTSAFALSEQ PAPDRSYGRM ATPTVSAVEA RLALLEDAPC
     LLFPSGMGAY GALMMAALKT GDRVLLLSDG YYAARALTET VLAPFGITMQ TCAAHDIATA
     PLDGIAMVIV ETPSNPGLDV IDIAALAERC HAVGARLVVD NTVCTPLLQQ PLDLGADAVI
     VSDTKAMGGH SDLLMGHVAS RDAGLMERLH ATRSLAGAIP GPFEAWLLLR GLETLDLRLA
     RMCENARAAL PILSASDKVS DVIYPAPHPQ TSDQGFLVGA TFADAPTADR FLEMAGFAPT
     TSFGGLHSSG DRRARWGDAV PAGFLRLSFG TEPTDRLMAD LARALDRA
//
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