UniProt: A0A090KST4

Database: UniProt
Entry: A0A090KST4_9BACI

LinkDB:  A0A090KST4_9BACI 
Original site:  A0A090KST4_9BACI

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (5)   
   EMBL (5)   
Protein domain (6)   
   InterPro (4)   
   Pfam (1)   
   PROSITE (1)   
All databases (18)   

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ID   A0A090KST4_9BACI        Unreviewed;       377 AA.
AC   A0A090KST4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Cystathionine gamma-lyase {ECO:0000313|EMBL:CEE01759.1};
DE            EC=4.4.1.1 {ECO:0000313|EMBL:CEE01759.1};
GN   Name=mccB {ECO:0000313|EMBL:CEE01759.1};
GN   ORFNames=B4064_2418 {ECO:0000313|EMBL:KIO65849.1}, B4065_3038
GN   {ECO:0000313|EMBL:KIO63254.1}, B4166_3024
GN   {ECO:0000313|EMBL:KIO63510.1}, B4167_2646
GN   {ECO:0000313|EMBL:KIO72870.1}, BT1A1_1937
GN   {ECO:0000313|EMBL:CEE01759.1};
OS   Caldibacillus thermoamylovorans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Caldibacillus.
OX   NCBI_TaxID=35841 {ECO:0000313|EMBL:CEE01759.1, ECO:0000313|Proteomes:UP000040576};
RN   [1] {ECO:0000313|EMBL:CEE01759.1, ECO:0000313|Proteomes:UP000040576}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Wibberg Daniel;
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000032071, ECO:0000313|Proteomes:UP000032076}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4064 {ECO:0000313|EMBL:KIO65849.1,
RC   ECO:0000313|Proteomes:UP000032078}, B4065
RC   {ECO:0000313|EMBL:KIO63254.1, ECO:0000313|Proteomes:UP000032071},
RC   B4166 {ECO:0000313|EMBL:KIO63510.1,
RC   ECO:0000313|Proteomes:UP000032097}, and B4167
RC   {ECO:0000313|EMBL:KIO72870.1, ECO:0000313|Proteomes:UP000032076};
RA   Krawcyk A.O., Berendsen E.M., Eijlander R.T., de Jong A., Wells-Bennik M.,
RA   Kuipers O.P.;
RT   "Draft Genome Sequences of Four Bacillus thermoamylovorans Strains,
RT   Isolated From Food Products.";
RL   Submitted (JAN-2015) 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|ARBA:ARBA00009077, ECO:0000256|RuleBase:RU362118}.
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DR   EMBL; CCRF01000061; CEE01759.1; -; Genomic_DNA.
DR   EMBL; JXLS01000085; KIO63254.1; -; Genomic_DNA.
DR   EMBL; JXLT01000110; KIO63510.1; -; Genomic_DNA.
DR   EMBL; JXLR01000055; KIO65849.1; -; Genomic_DNA.
DR   EMBL; JXLU01000080; KIO72870.1; -; Genomic_DNA.
DR   RefSeq; WP_034770473.1; NZ_JXLU01000080.1.
DR   AlphaFoldDB; A0A090KST4; -.
DR   STRING; 35841.B4167_2646; -.
DR   PATRIC; fig|35841.6.peg.298; -.
DR   eggNOG; COG0626; Bacteria.
DR   OrthoDB; 9803887at2; -.
DR   Proteomes; UP000032071; Unassembled WGS sequence.
DR   Proteomes; UP000032076; Unassembled WGS sequence.
DR   Proteomes; UP000032078; Unassembled WGS sequence.
DR   Proteomes; UP000032097; Unassembled WGS sequence.
DR   Proteomes; UP000040576; 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   CDD; cd00614; CGS_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; 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:SF92; CYSTATHIONINE GAMMA-SYNTHASE; 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.
DR   PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:CEE01759.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000040576}.
FT   MOD_RES         194
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   377 AA;  40978 MW;  27B0C7DFC311757C CRC64;
     MRKKTLMIHG GISRDEQTGA VSIPVSHAST FKQNGVGNFK YEYARTGNPT REALEAIIRD
     LEGGVAGFAF SSGMAAISAV MHLFKGGDHI ILTDDVYGGT FRLATKILNR YQIDVSFVDT
     SDAEQVRKAI QSNTKAIYIE TPTNPLLKVT NIREIAAIAK ENDLLVIVDN TFATPYWQNP
     LELGADIVLH SATKYLGGHS DVVAGVAVVG SDRLARELHF IQNSVGAVLG PDDSWLLIRG
     IKTLAIRMEE IEANTKAIAE FLQEHPKVRR VFYPGFPTHI GHEVHKSQAC GFGGMISFDV
     GSGELAEQVL AKTKIFTLAE SLGAVESLIS LPAKMTHASI PKERREQLGI TDGLIRISVG
     IEDVQDLIED LKTALDS
//

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