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Database: UniProt
Entry: L0DWH1_THIND
LinkDB: L0DWH1_THIND
Original site: L0DWH1_THIND 
ID   L0DWH1_THIND            Unreviewed;       394 AA.
AC   L0DWH1;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=Cystathionine gamma-synthase-like protein {ECO:0000313|EMBL:AGA33363.1};
GN   OrderedLocusNames=TVNIR_1701 {ECO:0000313|EMBL:AGA33363.1};
OS   Thioalkalivibrio nitratireducens (strain DSM 14787 / UNIQEM 213 / ALEN2).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Thioalkalivibrio.
OX   NCBI_TaxID=1255043 {ECO:0000313|EMBL:AGA33363.1, ECO:0000313|Proteomes:UP000010809};
RN   [1] {ECO:0000313|Proteomes:UP000010809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14787 / UNIQEM 213 / ALEN2
RC   {ECO:0000313|Proteomes:UP000010809};
RA   Tikhonova T.V., Pavlov A.R., Beletsky A.V., Mardanov A.V., Sorokin D.Y.,
RA   Ravin N.V., Popov V.O.;
RT   "Complete sequence of Thioalkalivibrio nitratireducens.";
RL   Submitted (DEC-2012) 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}.
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DR   EMBL; CP003989; AGA33363.1; -; Genomic_DNA.
DR   RefSeq; WP_015258491.1; NC_019902.2.
DR   AlphaFoldDB; L0DWH1; -.
DR   STRING; 1255043.TVNIR_1701; -.
DR   KEGG; tni:TVNIR_1701; -.
DR   PATRIC; fig|1255043.3.peg.1722; -.
DR   eggNOG; COG0626; Bacteria.
DR   HOGENOM; CLU_018986_2_3_6; -.
DR   OrthoDB; 9805807at2; -.
DR   Proteomes; UP000010809; Chromosome.
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.
DR   PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2}.
FT   MOD_RES         208
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   394 AA;  41510 MW;  0B4188B12DBC02EB CRC64;
     MNAKTQPALS TRCVHAGEAR DAHGSPHTPV YTTTTFAFPS TRALLDVVEG VKPGSLYTRY
     GLNPTIQSLE AKLASLEGAE AALAFSSGMG AEAALFLAHG RNGIVCLGDA YGGTLELLAD
     QLPQLGIRTA LLLGDEQERL DELLADGYGL VFLETPTNPV LEIFDIRALA RKAHAHGARL
     AVDNTFASPV NQQPLVLGAD FVIHSATKYL GGHSDLTAGA LMGPAEFVAP VAGWRKNLGT
     APAPETAAML ARSIRTLVVR VWQQNQNAQA IAEAMERHPR IRRVLYPGLA SHPGHAVAAE
     QMSGFGGMLM IEVDGDTAAT SAVVDRLQLF AIAPSLGGVE SLATQPVTTT HHGLSDAERE
     RRGISGSMIR LSVGLEDAQD LIADLEQALS APRG
//
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