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Database: UniProt
Entry: A0A1Q7F4M5_9CHLR
LinkDB: A0A1Q7F4M5_9CHLR
Original site: A0A1Q7F4M5_9CHLR 
ID   A0A1Q7F4M5_9CHLR        Unreviewed;       382 AA.
AC   A0A1Q7F4M5;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:OLC21911.1};
GN   ORFNames=AUH33_00735 {ECO:0000313|EMBL:OLC21911.1};
OS   Chloroflexi bacterium 13_1_40CM_68_21.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1805084 {ECO:0000313|EMBL:OLC21911.1, ECO:0000313|Proteomes:UP000185570};
RN   [1] {ECO:0000313|EMBL:OLC21911.1, ECO:0000313|Proteomes:UP000185570}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27843720;
RA   Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA   Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA   Banfield J.F.;
RT   "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT   heterotrophy are prevalent below the grass root zone.";
RL   PeerJ 4:E2687-E2687(2016).
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}.
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:OLC21911.1}.
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DR   EMBL; MNEO01000012; OLC21911.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q7F4M5; -.
DR   Proteomes; UP000185570; Unassembled WGS sequence.
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:SF15; CYSTATHIONINE GAMMA-LYASE; 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   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2}.
FT   MOD_RES         202
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   382 AA;  40567 MW;  1B2F48E4405E44D2 CRC64;
     MKSAARKHGF ETLAIHAGQD PEQATGAVVV PIFQTSTFAQ EAVGKNKGYE YARTGNPTRT
     ALETCLASLE GARWGLAFAS GMAASDAVAH LLSKGDHVVM TDDVYGGTYR LFARVFDRAG
     IGLTAVDMRK PDAVRRAMRA RTKLVWIETP SNPLLKVLDI GALAEMAHKA RALALVDNTF
     ASPYLQQPVK LGADVVLHST TKYLGGHSDV VGGALVGNDA ELRDRLAFLQ NAAGGVPGPF
     DAWLVLRGAK TLSLRMERHS ANAQAIAEWL AEHPRVTRVN YPGLASHPQH ALARRQMRAF
     GGMLSFELRG GEAAAKRAAA RTKIFALAES LGGVESLVEV PLAMTHGSVR GTKLAPPAGL
     VRLSVGIETV DDLIADLAQA IG
//
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