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Database: UniProt
Entry: A0A089JPC8_9BACL
LinkDB: A0A089JPC8_9BACL
Original site: A0A089JPC8_9BACL 
ID   A0A089JPC8_9BACL        Unreviewed;       390 AA.
AC   A0A089JPC8;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:AIQ22839.1};
DE            EC=2.5.1.48 {ECO:0000313|EMBL:AIQ22839.1};
GN   ORFNames=H70737_08225 {ECO:0000313|EMBL:AIQ22839.1};
OS   Paenibacillus sp. FSL H7-0737.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1536775 {ECO:0000313|EMBL:AIQ22839.1, ECO:0000313|Proteomes:UP000029519};
RN   [1] {ECO:0000313|EMBL:AIQ22839.1, ECO:0000313|Proteomes:UP000029519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL H7-0737 {ECO:0000313|EMBL:AIQ22839.1,
RC   ECO:0000313|Proteomes:UP000029519};
RA   den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT   "Comparative genomics of the Paenibacillus odorifer group.";
RL   Submitted (AUG-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}.
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DR   EMBL; CP009279; AIQ22839.1; -; Genomic_DNA.
DR   RefSeq; WP_042186212.1; NZ_CP009279.1.
DR   AlphaFoldDB; A0A089JPC8; -.
DR   KEGG; paej:H70737_08225; -.
DR   eggNOG; COG0626; Bacteria.
DR   HOGENOM; CLU_018986_2_0_9; -.
DR   Proteomes; UP000029519; Chromosome.
DR   GO; GO:0003962; F:cystathionine gamma-synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102028; F:cystathionine gamma-synthase activity (acts on O-phosphohomoserine); IEA:UniProtKB-EC.
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: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:UP000029519};
KW   Transferase {ECO:0000313|EMBL:AIQ22839.1}.
FT   MOD_RES         199
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   390 AA;  42528 MW;  21E21040D9123388 CRC64;
     MDDKLRIESR LAQIGSQEDP ATGAINFPIY NATAFRHPKL GQSTGFDYSR TKSPTRSVLE
     NAAAELESGD AGFACSSGMA AIQTVLTLFA QGDHLIVSLD LYGGTYRLLE RIMSKFGITA
     SYVDTNDLDA LETSRRPNTK AVFIETPTNP LMMITDIEAV CTWARHHGLL SIVDNTLLTP
     FFQRPIELGA DIVVHSATKY LGGHNDVLAG LIVSKGVELS AELAILHNSI GAVLGPTDSY
     QLMRGLKTLA LRMERHESNA LAIAHYLLEH PAIAEVFHPG LPDHPGHEIQ NRQSSGNTGI
     FSFKLKDARY VEPLLRHIRL IAFAESLGGV ESLMTYPAVQ THADIPVEIR NAVGVDDRLL
     RFSVGIEHAE DLIADLSQAL EAARAEIESK
//
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