ID A0A101IH93_9BACT Unreviewed; 385 AA.
AC A0A101IH93;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Cystathionine beta-lyases/cystathionine gamma-synthase {ECO:0000313|EMBL:KUK95222.1};
GN ORFNames=XE05_0198 {ECO:0000313|EMBL:KUK95222.1};
OS Thermotogales bacterium 46_20.
OC Bacteria; Thermotogota; Thermotogae; Thermotogales.
OX NCBI_TaxID=1635293 {ECO:0000313|EMBL:KUK95222.1, ECO:0000313|Proteomes:UP000054930};
RN [1] {ECO:0000313|Proteomes:UP000054930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
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:KUK95222.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LGGZ01000003; KUK95222.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101IH93; -.
DR Proteomes; UP000054930; 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: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; 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:KUK95222.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2}.
FT MOD_RES 203
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 385 AA; 41810 MW; 431AEFB710547AB0 CRC64;
MKRSRGFNTE AVHAGESSNR FADAVTVPVF QTSNFLMNDE KYSSPDNVNN VYTRLGNPTI
GALVEKLNAL CNASFGVFFS SGMGAISAVL GSFLKKEDSI LFCRPIYGGT SALLDEFRHA
GIRMDSFTPS SIDRITSLID HTTRIIYTET LTNPSSQLVD IEKIATIAES HNILLVVDNT
FLSPYNFTAL DHGAHIEVHS LSKYINGHSD VVAGYACTND QAVYERVRSM MTMIGSNGNP
ADAFLVMRGA KTLGLRMQAH NTNGEVIARF LSSSPVIKCV QHPSLVKDLP ACYRNCPGYG
GMIYLEFFRE EDAMKFIRSA KLLTEATSLG GVESLVTMPS LTSHSSSARD DLTEAGISSS
GVRLSLGVED SEDLLKSISE VLSVL
//
