ID T0T5F1_9STRE Unreviewed; 364 AA.
AC T0T5F1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:EQC68680.1};
DE EC=2.5.1.48 {ECO:0000313|EMBL:EQC68680.1};
GN ORFNames=HSISB1_1848 {ECO:0000313|EMBL:EQC68680.1};
OS Streptococcus sp. HSISB1.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1316409 {ECO:0000313|EMBL:EQC68680.1};
RN [1] {ECO:0000313|EMBL:EQC68680.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HSISB1 {ECO:0000313|EMBL:EQC68680.1};
RA Van den Bogert B., Boekhorst J., Herrmann R., Smid E.J., Zoetendal E.G.,
RA Kleerebezem M.;
RT "Comparative Genomics Analysis of Streptococcus Isolates from the Human
RT Small Intestine Reveals their Adaptation to a Highly Dynamic Ecosystem.";
RL PLoS ONE 8:E83418-E83418(2013).
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:EQC68680.1}.
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DR EMBL; ASKA01000036; EQC68680.1; -; Genomic_DNA.
DR AlphaFoldDB; T0T5F1; -.
DR PATRIC; fig|1316409.3.peg.1545; -.
DR HOGENOM; CLU_018986_2_0_9; -.
DR Proteomes; UP000015934; 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 Transferase {ECO:0000313|EMBL:EQC68680.1}.
FT MOD_RES 197
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 364 AA; 40022 MW; 95C3A050A6E24853 CRC64;
MKSDCRLATI LAHAGIKSDE ATGALAAPIH FSTTYQHPEF GQSTGFDYTR TKNPTRATLE
KTLAAIENAD YALATSSGMS AIVLALEIFP VGAKVVAARD LYGGSFRWFN DKEKEGRFNF
TYVNNETDLL TAISEETDLV YLETPTNPLM IEFDIAKVAK VAHKNGAKLI VDNTFYSPIY
QNPITLGADI VVHSATKYLA GHNDVLAGVV ITSDKAIYDK LFYNLNTTGP TLSPFDSYML
MRGLKTLKLR MEKATENAQE IVAFLKNSSA VKEVLYTGKG GMISFKVVDE EKIPHIINSL
EIITFAESLG GVESLITYPR TQTHADIPED VRLSYGLTND LLRLSIGIED VDDLIEDLKN
ALED
//