ID Q5M4H0_STRT2 Unreviewed; 437 AA.
AC Q5M4H0;
DT 01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 01-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE SubName: Full=O-acetylhomoserine sulfhydrylase {ECO:0000313|EMBL:AAV60647.1};
GN Name=cysD {ECO:0000313|EMBL:AAV60647.1};
GN OrderedLocusNames=stu0987 {ECO:0000313|EMBL:AAV60647.1};
OS Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=264199 {ECO:0000313|EMBL:AAV60647.1, ECO:0000313|Proteomes:UP000001170};
RN [1] {ECO:0000313|EMBL:AAV60647.1, ECO:0000313|Proteomes:UP000001170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-250 / LMG 18311 {ECO:0000313|Proteomes:UP000001170};
RX PubMed=15543133; DOI=10.1038/nbt1034;
RA Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D.,
RA Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M.,
RA Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D.,
RA Hancy F., Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.;
RT "Complete sequence and comparative genome analysis of the dairy bacterium
RT Streptococcus thermophilus.";
RL Nat. Biotechnol. 22:1554-1558(2004).
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}.
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DR EMBL; CP000023; AAV60647.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5M4H0; -.
DR STRING; 264199.stu0987; -.
DR KEGG; stl:stu0987; -.
DR eggNOG; COG2873; Bacteria.
DR HOGENOM; CLU_018986_4_0_9; -.
DR Proteomes; UP000001170; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; 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; IPR006235; OAc-hSer/O-AcSer_sulfhydrylase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR01326; OAH_OAS_sulfhy; 1.
DR PANTHER; PTHR43797; HOMOCYSTEINE/CYSTEINE SYNTHASE; 1.
DR PANTHER; PTHR43797:SF2; HOMOCYSTEINE_CYSTEINE SYNTHASE; 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:UP000001170}.
FT MOD_RES 219
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 437 AA; 47509 MW; A1A14B756644ABF0 CRC64;
MKATFVLEDT HMSREFSFET LQLHAGQTPD KETKSRAVPI YQTTSYVFDD AQEGEDLFAL
RKPGNIYTRI TNPTVAVLEE RIAALEGGVG ALATASGMAA ITYAILGLAH AGDHVVAATT
LYGGTFNLLK ETLPRYGITT TFVDVDNPEE IEAAIKDNTK LVLIESLGNP LINIPDFEKI
AEIAHSHKIP LVADNTFGTP YLINVISHGV DIVLHSATKF IGGHGTTIGG LIVDSGKFDW
EASGKFPQLV DEDPSYHNIS YTRDVGPAAF VTALRTQLLR DTGAALAPFN AFLLLQGLET
LSLRVERHVE NTKKIVDFLE NHPKVEKVNY PGLPSSPYYD LAQKYFSKGP GSIFTFHVKG
GQDEARTIID NLEIFSDLAN VADAKSLVVH PATTTHQQLA EADLLACGVT PNQIRISVGL
ENADDLIEDL KLALDKI
//
