ID I2F5K2_9BACT Unreviewed; 380 AA.
AC I2F5K2;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE SubName: Full=Cystathionine beta-lyase/cystathionine gamma-synthase {ECO:0000313|EMBL:AFK07205.1};
DE Flags: Precursor;
GN ORFNames=Theba_1529 {ECO:0000313|EMBL:AFK07205.1};
OS Mesotoga prima MesG1.Ag.4.2.
OC Bacteria; Thermotogota; Thermotogae; Kosmotogales; Kosmotogaceae; Mesotoga.
OX NCBI_TaxID=660470 {ECO:0000313|EMBL:AFK07205.1, ECO:0000313|Proteomes:UP000002881};
RN [1] {ECO:0000313|EMBL:AFK07205.1, ECO:0000313|Proteomes:UP000002881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=mesG1.Ag.4.2 {ECO:0000313|Proteomes:UP000002881};
RX PubMed=22798451;
RA Zhaxybayeva O., Swithers K.S., Foght J., Green A.G., Bruce D., Detter C.,
RA Han S., Teshima H., Han J., Woyke T., Pitluck S., Nolan M., Ivanova N.,
RA Pati A., Land M.L., Dlutek M., Doolittle W.F., Noll K.M., Nesbo C.L.;
RT "Genome Sequence of the Mesophilic Thermotogales Bacterium Mesotoga prima
RT MesG1.Ag.4.2 Reveals the Largest Thermotogales Genome To Date.";
RL Genome Biol. Evol. 4:700-708(2012).
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 ---------------------------------------------------------------------------
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; CP003532; AFK07205.1; -; Genomic_DNA.
DR RefSeq; WP_014731123.1; NC_017934.1.
DR AlphaFoldDB; I2F5K2; -.
DR STRING; 660470.Theba_1529; -.
DR KEGG; mpg:Theba_1529; -.
DR eggNOG; COG0626; Bacteria.
DR HOGENOM; CLU_018986_2_0_0; -.
DR Proteomes; UP000002881; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 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; 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:AFK07205.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000002881};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 65..89
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT MOD_RES 198
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 380 AA; 41261 MW; 3F8FE9CEE596C10C CRC64;
MRGFNTRAIH AGEEKKINDA VSTPIFQTSN FLADDVKYMD ESSEVLYTRV GNPSIGVVER
KLSDLFGGTG GVFFSSGMGA ITTVFLSILK SGMNLVISRN IYGGTQSLIS DLPGMGVEIR
RFDQSRIDEL ETLIDDKTGI VYVESMSNPD LILSDIEGIA RITREKEAVL VVDNTFLSPY
NFRPLEYGAD VDIQSLSKYV NGHSDVIAGF AAFKDSGLEK RVRKVMIKLG TNGAPFDAFL
VGRGAKTLGP RMELHNRNAR EVAEFLSKNP KVLRVSYPSL KASVPACFSE CRGFGGVVYL
ELESLSAAKS FIRRSELFLE ATSLAGVESL ATIPVLTSHA SLSAEQLRDA GLSEGGVRLS
VGIEDLEDLL SDLDFAMKGI
//
