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Database: UniProt
Entry: S3AKH8_BIFBR
LinkDB: S3AKH8_BIFBR
Original site: S3AKH8_BIFBR 
ID   S3AKH8_BIFBR            Unreviewed;       394 AA.
AC   S3AKH8;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Cystathionine gamma-synthase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=HMPREF1482_00639 {ECO:0000313|EMBL:EPD76854.1};
OS   Bifidobacterium breve HPH0326.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1203540 {ECO:0000313|EMBL:EPD76854.1, ECO:0000313|Proteomes:UP000014395};
RN   [1] {ECO:0000313|EMBL:EPD76854.1, ECO:0000313|Proteomes:UP000014395}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HPH0326 {ECO:0000313|EMBL:EPD76854.1,
RC   ECO:0000313|Proteomes:UP000014395};
RG   The Broad Institute Genomics Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T.M., Dover J., Dai D.,
RA   Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Bifidobacterium breve HPH0326.";
RL   Submitted (MAY-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|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:EPD76854.1}.
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DR   EMBL; ATCB01000001; EPD76854.1; -; Genomic_DNA.
DR   RefSeq; WP_016462326.1; NZ_KE150453.1.
DR   AlphaFoldDB; S3AKH8; -.
DR   PATRIC; fig|1203540.3.peg.624; -.
DR   HOGENOM; CLU_018986_2_0_11; -.
DR   Proteomes; UP000014395; 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         209
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   394 AA;  41719 MW;  B10D9C9B552E96E9 CRC64;
     MSAEYNAKFA NTAVATRAIH AGQEPDPTTG AVVTPIYATS TFKQDGVLGL RGGHDYSRSI
     NPTRTSFDEQ LAAVEGAKYA LSFSSGLAAI DVLLRSTIKP GDNILLGNDV YGGTYRLLSK
     VFVPWGVGLD VVDITDTAAV EAALAAKSYK YVWVETPSNP LLNITDIAVT SEVAHKYGTK
     VAVDNTFASP ALQHPLDDGA DVVVYSTTKY IGGHSDVVGG AVVLNDEETR EQVAFLQNAA
     GAVPSPFDSF LDIRGLKTLD LRVKRHSANA LKVAEWLESQ PADVIERVWY PGLESHPGHD
     IAARQMHGGF GGVLSVQLAG GAEAAKKFVD YTEIFTLAES LGGVESLIEV PAAMTHASVA
     GTTLQVPGNL VRISVGIENA DDLIADLKQA LDRL
//
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