ID A0A0R1VNT6_9LACO Unreviewed; 445 AA.
AC A0A0R1VNT6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=O-acetylhomoserine O-acetylserine sulfhydrylase {ECO:0000313|EMBL:KRM07087.1};
GN ORFNames=FC89_GL000401 {ECO:0000313|EMBL:KRM07087.1};
OS Liquorilactobacillus ghanensis DSM 18630.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Liquorilactobacillus.
OX NCBI_TaxID=1423750 {ECO:0000313|EMBL:KRM07087.1, ECO:0000313|Proteomes:UP000051451};
RN [1] {ECO:0000313|EMBL:KRM07087.1, ECO:0000313|Proteomes:UP000051451}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18630 {ECO:0000313|EMBL:KRM07087.1,
RC ECO:0000313|Proteomes:UP000051451};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRM07087.1}.
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DR EMBL; AZGB01000009; KRM07087.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R1VNT6; -.
DR STRING; 1423750.FC89_GL000401; -.
DR PATRIC; fig|1423750.3.peg.410; -.
DR Proteomes; UP000051451; Unassembled WGS sequence.
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:UP000051451}.
FT MOD_RES 227
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 445 AA; 48264 MW; 242C486F7CF2FB16 CRC64;
MHICITGIFY YQKIKEEIKM VAEDFHFETL QVHAGQTVDE TGARAVPIYQ TTSYVFKDAQ
QAADRFGLKD PGNIYTRLTN PTTAVVDQRV AALEHGTSGV TLATGAAAIS AAITNIAGQG
DEIVAASTLY GGTYNLFNVT FPKLGIKTHF VNSDDPQNFA AAINEHTKAL YVETIGNPDI
NLVDLEAIAE IAHAHQLLLI SDNTFASPYL YRPLEHGADI VIESATKFIG GHGTTMGGVI
VENDQFDYRA SQRYPEFTTP DPQYSGLIFA DLKGGAFTTK VRAEGLRDTG GTISPFNSFL
LLQGLETLSL RVERHVANTR KVIAFLQDHP KVAWIKYPEL ADSPYHSLAA RDFPKGVGSI
FTLGLTGGEQ AGKALIEHLK IFSLLANVGD AKSLIIHPAS TTHAQLNEAE LRQAGITPDL
IRVSIGIENA DDLIADLKQA LEKID
//
