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Database: UniProt
Entry: R4KH20_CLOPA
LinkDB: R4KH20_CLOPA
Original site: R4KH20_CLOPA 
ID   R4KH20_CLOPA            Unreviewed;       436 AA.
AC   R4KH20;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=O-acetylhomoserine sulfhydrylase {ECO:0000313|EMBL:AGK98910.1};
GN   ORFNames=Clopa_4180 {ECO:0000313|EMBL:AGK98910.1};
OS   Clostridium pasteurianum BC1.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=86416 {ECO:0000313|EMBL:AGK98910.1, ECO:0000313|Proteomes:UP000013523};
RN   [1] {ECO:0000313|EMBL:AGK98910.1, ECO:0000313|Proteomes:UP000013523}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BC1 {ECO:0000313|EMBL:AGK98910.1,
RC   ECO:0000313|Proteomes:UP000013523};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Dunn J.,
RA   Taghavi S., Francis A., van der Lelie D., Woyke T.;
RT   "Complete sequence of chromosome of Clostridium pasteurianum BC1.";
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
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; CP003261; AGK98910.1; -; Genomic_DNA.
DR   RefSeq; WP_015617184.1; NC_021182.1.
DR   AlphaFoldDB; R4KH20; -.
DR   STRING; 86416.Clopa_4180; -.
DR   KEGG; cpas:Clopa_4180; -.
DR   PATRIC; fig|86416.3.peg.4184; -.
DR   eggNOG; COG2873; Bacteria.
DR   HOGENOM; CLU_018986_4_0_9; -.
DR   OrthoDB; 9780685at2; -.
DR   Proteomes; UP000013523; 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   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.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013523}.
FT   MOD_RES         210
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   436 AA;  48252 MW;  8E3069DB567AA10B CRC64;
     MANEELKFDT LKIRGAYNSA EHNYAASVPI YETAAFDLGS TERAGNLFSF SEPGFIYTRV
     GNPTTNVLEQ RVAALDGAAG AVAVGSGMAA VTYTLFNVAE NGGRILTTPY LYGGTIDSFK
     KIYPKFGVDI DKSENFHNPE ELAKDIKPDT KAIFVESISN PNAVIADLEA LAKVAHDHDI
     PLIVDNTFAT PYLLNPIKYG ADIVIYSATK ALGGHGNSIA GLILESGKFN WGNGKFPQFQ
     EPDYTLRDSE GKSRTFLDVF PEFPFTWRIR KNYLAYFGAA LSPFNSYLTL LGIETLSERI
     QKQVENTKKI IYYLEDNDKV EWIKHPSAKG NPYRELAEKY VPKGAGSIFS FGFKGTDEQI
     NKFLNAIKLF NYHTNVGDVR SLIINSPKTT HGELTREEQE FSDIAPNTIR ISVGLEDPQD
     LIADLDQAFK ASSKNN
//
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