ID K6SYN7_9CLOT Unreviewed; 429 AA.
AC K6SYN7;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=OAH/OAS sulfhydrylase {ECO:0000313|EMBL:EKQ51508.1};
GN ORFNames=A370_04811 {ECO:0000313|EMBL:EKQ51508.1};
OS Clostridium sp. Maddingley MBC34-26.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1196322 {ECO:0000313|EMBL:EKQ51508.1, ECO:0000313|Proteomes:UP000001325};
RN [1] {ECO:0000313|EMBL:EKQ51508.1, ECO:0000313|Proteomes:UP000001325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Maddingley MBC34-26 {ECO:0000313|Proteomes:UP000001325};
RX PubMed=23405323;
RA Rosewarne C.P., Greenfield P., Li D., Tran-Dinh N., Bradbury M.I.,
RA Midgley D.J., Hendry P.;
RT "Draft Genome Sequence of Clostridium sp. Maddingley, Isolated from Coal-
RT Seam Gas Formation Water.";
RL Genome Announc. 1:E00081-12(2013).
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:EKQ51508.1}.
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DR EMBL; ALXI01000156; EKQ51508.1; -; Genomic_DNA.
DR AlphaFoldDB; K6SYN7; -.
DR STRING; 1196322.A370_04811; -.
DR PATRIC; fig|1196322.3.peg.4676; -.
DR eggNOG; COG2873; Bacteria.
DR Proteomes; UP000001325; 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:UP000001325}.
FT MOD_RES 212
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 429 AA; 46465 MW; 1EBB39D4421F0C8E CRC64;
MSNQERKLKF ETLQLHVGQE KPDSATDARA VPIYQTTSYV FRNSAHAAAR FGLADAGNIY
GRVTNSTQDV LESRVAALEG GIAGLAVASG AAAITYAIQN ITHAGDHIVA AKTIYGGSYN
LLAHTLPTYG VSTTFVDPDD LSNFENAIQD NTKALFIETL GNPNSNVIDV DAVAEIAHKY
KIPLIVDNTF GTPYLFRPIE HGADIVVHSA TKFIGGHGTS LGGIIVDSGK FDWIGSGKFP
QLTEADPSYH GIKFIEAAGQ AAYIIRARTI LLRDTGASIS PFNAFILLQG LETLSLRVER
HVENTVKVVE FLKNHPQVES VNHPSLTESK YNDLYKKYFP NGAGSIFTFE IKGGAKEAQD
FIDRLQIFSL LANVADVKSL VIHPASTTHS QLSEEELLDQ GIKPNTIRLS IGTEHIDDII
YDLSQALGA
//
