ID Q8DPM6_STRR6 Unreviewed; 371 AA.
AC Q8DPM6;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE SubName: Full=O-acetylhomoserine sulfhydrylase, truncation {ECO:0000313|EMBL:AAK99898.1};
DE EC=2.5.1.49 {ECO:0000313|EMBL:AAK99898.1};
GN OrderedLocusNames=spr1095 {ECO:0000313|EMBL:AAK99898.1};
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101 {ECO:0000313|EMBL:AAK99898.1, ECO:0000313|Proteomes:UP000000586};
RN [1] {ECO:0000313|EMBL:AAK99898.1, ECO:0000313|Proteomes:UP000000586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6 {ECO:0000313|Proteomes:UP000000586};
RX PubMed=11544234; DOI=10.1128/JB.183.19.5709-5717.2001;
RA Hoskins J.A., Alborn W.Jr., Arnold J., Blaszczak L., Burgett S.,
RA DeHoff B.S., Estrem S., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A., LaGace R., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S., McHenney M.,
RA McLeaster K., Mundy C., Nicas T.I., Norris F.H., O'Gara M., Peery R.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C., Baltz R.H., Jaskunas S.Richard.,
RA Rosteck P.R.Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
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; AE007317; AAK99898.1; -; Genomic_DNA.
DR PIR; F98008; F98008.
DR AlphaFoldDB; Q8DPM6; -.
DR STRING; 171101.spr1095; -.
DR KEGG; spr:spr1095; -.
DR eggNOG; COG2873; Bacteria.
DR HOGENOM; CLU_018986_4_0_9; -.
DR Proteomes; UP000000586; Chromosome.
DR GO; GO:0003961; F:O-acetylhomoserine aminocarboxypropyltransferase activity; 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; 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:UP000000586};
KW Transferase {ECO:0000313|EMBL:AAK99898.1}.
FT MOD_RES 153
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 371 AA; 40246 MW; 4FF2C4FEF7FA0281 CRC64;
MRKPGNIYTR ITNPTTAALE GGVEALATAS GMTAVTYTIL ALAHAGEHVV AASTIYGGTF
NLLKEPLPRY GITTTFVDVD NLEEVEAAIK DNTKLVLIET LGNPLINIPD LEKLAEIAHK
HQIPLVSDNT FATPYLINVF SHGVDIAIHS ATKFIGGHGT TIGGIIVDSG RFDWTASGKF
PQFVDESPSC HNLSYTHDVG AAAFIIAVRV QLLRDTGAAL SPFNAFLLLQ RLETLSLRVE
RHVQNAETIV DFLVNHPKVE KVNYPKLADS PYYALAEKYL PKGVGSIFTF HVKGDEEEAR
KVIDNLEIFS DLANAADAKS LVVHPATITH GQLSEKDLEA AGVTPNQIHL SIGLENVEDL
IEDLRLALEK I
//
