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Database: UniProt
Entry: A0A0J8DBG4_CLOCY
LinkDB: A0A0J8DBG4_CLOCY
Original site: A0A0J8DBG4_CLOCY 
ID   A0A0J8DBG4_CLOCY        Unreviewed;       430 AA.
AC   A0A0J8DBG4;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Putative cysteine desulfurase Csd {ECO:0000313|EMBL:KMT23182.1};
DE            EC=2.8.1.7 {ECO:0000313|EMBL:KMT23182.1};
GN   Name=csd {ECO:0000313|EMBL:KMT23182.1};
GN   ORFNames=CLCY_6c00630 {ECO:0000313|EMBL:KMT23182.1};
OS   Clostridium cylindrosporum DSM 605.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1121307 {ECO:0000313|EMBL:KMT23182.1, ECO:0000313|Proteomes:UP000036756};
RN   [1] {ECO:0000313|EMBL:KMT23182.1, ECO:0000313|Proteomes:UP000036756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 605 {ECO:0000313|EMBL:KMT23182.1,
RC   ECO:0000313|Proteomes:UP000036756};
RA   Poehlein A., Schiel-Bengelsdorf B., Bengelsdorf F., Daniel R., Duerre P.;
RT   "Draft genome sequence of the purine-degrading Clostridium cylindrosporum
RT   HC-1 (DSM 605).";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-
CC         alanine; Xref=Rhea:RHEA:43892, Rhea:RHEA-COMP:14737, Rhea:RHEA-
CC         COMP:14739, ChEBI:CHEBI:29917, ChEBI:CHEBI:35235, ChEBI:CHEBI:57972,
CC         ChEBI:CHEBI:64428; EC=2.8.1.7;
CC         Evidence={ECO:0000256|ARBA:ARBA00001357};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU004504};
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. Csd subfamily.
CC       {ECO:0000256|ARBA:ARBA00010447}.
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:KMT23182.1}.
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DR   EMBL; LFVU01000002; KMT23182.1; -; Genomic_DNA.
DR   RefSeq; WP_048569267.1; NZ_LFVU01000002.1.
DR   AlphaFoldDB; A0A0J8DBG4; -.
DR   STRING; 1121307.CLCY_6c00630; -.
DR   PATRIC; fig|1121307.3.peg.2195; -.
DR   OrthoDB; 9804366at2; -.
DR   Proteomes; UP000036756; Unassembled WGS sequence.
DR   GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
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; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43586; CYSTEINE DESULFURASE; 1.
DR   PANTHER; PTHR43586:SF8; CYSTEINE DESULFURASE 1, CHLOROPLASTIC; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000036756};
KW   Transferase {ECO:0000313|EMBL:KMT23182.1}.
FT   DOMAIN          29..417
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   430 AA;  48107 MW;  84E0C9B43595F21A CRC64;
     MNKKLDYRKL FAGINMPVAL EDGRCVVPIN FDNAATTPPF KCVNNMIIQN ILMYGSIGRG
     KGQKSEYCTD AYEEAREFIL DFFNLSNRKD YTVIYVKNAT EGINLLARSL IKESDEVVLT
     TRMEHHANDI PWRYVSKVEY IDVDENGKID INDIEKKLKN LKGKVKFVSI SGASNVTGYI
     NDINKIAQIT HKYGAKIVVD AAQLIAHRAI NMAGNENDDH IDFMTFSGHK LYAPFGSGVV
     VGLREAFNDG NLFLYGGGAV EAVLDDNVYW QKSPGKYEAG TPNFIGVIAL VTAMKSLISI
     GFDNIKTHED ELRDHAIKKL SNIDRIVLYG DSKCTERLGV VPFNIEGVGH NIVAERLADY
     RAIAVRHGGF CAHSYVRRLL GISNEKAYNY IINGVDMPGM VRASFGLYNT TEEIDEFIDV
     LKKIITRHIK
//
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