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Database: UniProt
Entry: A0A0B2AJI1_9MICC
LinkDB: A0A0B2AJI1_9MICC
Original site: A0A0B2AJI1_9MICC 
ID   A0A0B2AJI1_9MICC        Unreviewed;       365 AA.
AC   A0A0B2AJI1;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:KHL01981.1};
GN   ORFNames=LK10_13960 {ECO:0000313|EMBL:KHL01981.1};
OS   Sinomonas humi.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Sinomonas.
OX   NCBI_TaxID=1338436 {ECO:0000313|EMBL:KHL01981.1, ECO:0000313|Proteomes:UP000030982};
RN   [1] {ECO:0000313|EMBL:KHL01981.1, ECO:0000313|Proteomes:UP000030982}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MUSC 117 {ECO:0000313|EMBL:KHL01981.1,
RC   ECO:0000313|Proteomes:UP000030982};
RA   Lee L.-H.;
RT   "Genome sequence of Sinomonas sp. MUSC 117.";
RL   Submitted (SEP-2014) 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}.
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:KHL01981.1}.
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DR   EMBL; JTDL01000134; KHL01981.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B2AJI1; -.
DR   STRING; 1338436.LK10_13960; -.
DR   Proteomes; UP000030982; Unassembled WGS sequence.
DR   GO; GO:0016846; F:carbon-sulfur lyase activity; IEA:UniProt.
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:SF93; CYSTATHIONINE GAMMA-LYASE-RELATED; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030982}.
FT   MOD_RES         188
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   365 AA;  37811 MW;  433660DCC4D61BBB CRC64;
     MAAGRPERGH DTPVNPSVVF SSTFVGLGSV GEGARGYARF SNPTWEPFEE AVARLEGAEI
     PALLFSSGMA AVAAALSLVP VGGVLVAPAH AYSGTLGLAQ AKGVRGELEL RSVDIADTEA
     TVAALDGADV LWVESPTNPM MEVADLPALT AAAHAAGALV VVDNTFSTPL GQRPLSVGAD
     VVVHSATKYL AGHSDVLLGL AVTADDEIRA RLLGHRTLHG AIAGPMEAWL GLRGLRTLAL
     RVERSQATAA ELARRLEGHP AVRRTRYPGL VSDPGHERAA AQFDGFGSII SIELDDAAAA
     DALVAGLALW LPATSLGGVE STIERRRRHV AEPATVPEGL VRLSVGIENV DDLWADLAQG
     LDALV
//
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