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Database: UniProt
Entry: A0A0A5GP04_9BACI
LinkDB: A0A0A5GP04_9BACI
Original site: A0A0A5GP04_9BACI 
ID   A0A0A5GP04_9BACI        Unreviewed;       374 AA.
AC   A0A0A5GP04;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:KGX92963.1};
GN   ORFNames=N781_13895 {ECO:0000313|EMBL:KGX92963.1};
OS   Pontibacillus halophilus JSM 076056 = DSM 19796.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pontibacillus.
OX   NCBI_TaxID=1385510 {ECO:0000313|EMBL:KGX92963.1, ECO:0000313|Proteomes:UP000030528};
RN   [1] {ECO:0000313|EMBL:KGX92963.1, ECO:0000313|Proteomes:UP000030528}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JSM 076056 {ECO:0000313|EMBL:KGX92963.1,
RC   ECO:0000313|Proteomes:UP000030528};
RA   Huang J., Wang G.;
RL   Submitted (AUG-2013) 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:KGX92963.1}.
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DR   EMBL; AVPE01000004; KGX92963.1; -; Genomic_DNA.
DR   RefSeq; WP_026800042.1; NZ_AVPE01000004.1.
DR   AlphaFoldDB; A0A0A5GP04; -.
DR   STRING; 1385510.GCA_000425205_01610; -.
DR   eggNOG; COG0626; Bacteria.
DR   OrthoDB; 9803887at2; -.
DR   Proteomes; UP000030528; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:UniProt.
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; 2.
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:SF91; CYSTATHIONINE GAMMA-SYNTHASE; 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:UP000030528}.
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         198
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   374 AA;  41292 MW;  A62B5AD48C572F17 CRC64;
     MSNHHILTKL AQTGNRSETT TGAVNPPIYL STAYRHEGIG QSTGYDYTRT GNPTRAVLEQ
     SIADLEGGES GFAFSSGMAA IQATFGLFEP GDEFIVTQDV YGGSYRLFEN QLKKSGLSFN
     YVNSSNPKDF EQAITDKTKG FFIETPTNPL MTEIDVQQMS EIAAEHELLL IVDNTFYTPY
     LQRPIELGAD LVIHSATKYL GGHNDVLAGL VVSRHEALSE QLASEQNATG AVLSPFDCWL
     LMRGMKTLGL RMSQHEENAK LVAAFLEHNP YVTDVLYPGQ GGMLSFRVES EEAIPILLES
     FRLISFAESL GGTETFITYP ATQTHMDIPE EIRSNYGVCN RLLRLSVGLE YSEDLMKDLK
     EALEAAHKGV EVHE
//
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