ID Q8DST4_STRMU Unreviewed; 364 AA.
AC Q8DST4;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=Cystathionine gamma-synthase possible bifunctional enzyme {ECO:0000313|EMBL:AAN59314.1};
GN Name=metB {ECO:0000313|EMBL:AAN59314.1};
GN OrderedLocusNames=SMU_1675 {ECO:0000313|EMBL:AAN59314.1};
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007 {ECO:0000313|EMBL:AAN59314.1, ECO:0000313|Proteomes:UP000002512};
RN [1] {ECO:0000313|EMBL:AAN59314.1, ECO:0000313|Proteomes:UP000002512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159 {ECO:0000313|Proteomes:UP000002512};
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H., Lin S., Qian Y., Li S., Zhu H.,
RA Najar F., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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; AE014133; AAN59314.1; -; Genomic_DNA.
DR RefSeq; NP_722008.1; NC_004350.2.
DR RefSeq; WP_002262596.1; NC_004350.2.
DR AlphaFoldDB; Q8DST4; -.
DR STRING; 210007.SMU_1675; -.
DR KEGG; smu:SMU_1675; -.
DR PATRIC; fig|210007.7.peg.1497; -.
DR eggNOG; COG0626; Bacteria.
DR HOGENOM; CLU_018986_2_1_9; -.
DR OrthoDB; 9780685at2; -.
DR PhylomeDB; Q8DST4; -.
DR Proteomes; UP000002512; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000002512};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT MOD_RES 197
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 364 AA; 40239 MW; 483C92F36831B97F CRC64;
MTEDYKLDTI LAHAGINTDK TTGALTAPIH LSTTYQHPQF GQSTGFDYTR TKNPTRTVLE
ETLAKIEKAK YALVTSSGMA ALVLLFTGFP IGSKVVAARD LYGGSFRWFN EQEKAGRFSF
VYTNTETDMI AAISDETDYV FIETPTNPLM IEFDISKVAQ AAHKHGAKVI VDNTFYSPIY
QNPLVLGADV VLHSATKYLS GHNDVLAGVL MTSDQEIYDK LFYDQNTTGP TLSPLDTYLL
MRGLKTLKLR MEKATQNAKT VVAYLEKSPA VKEVLYTGKG GMISFKVVDE KKIPQILNHL
QLFTFAESLG GVESLITYPA TQTHLDIPEE VRHSYGLTDD LLRLSIGIED AEDLIDDLKA
ALEA
//
