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Database: UniProt
Entry: A0A238W0N8_9FLAO
LinkDB: A0A238W0N8_9FLAO
Original site: A0A238W0N8_9FLAO 
ID   A0A238W0N8_9FLAO        Unreviewed;       412 AA.
AC   A0A238W0N8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE            EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN   ORFNames=SAMN06265376_101580 {ECO:0000313|EMBL:SNR40112.1};
OS   Dokdonia pacifica.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Dokdonia.
OX   NCBI_TaxID=1627892 {ECO:0000313|EMBL:SNR40112.1, ECO:0000313|Proteomes:UP000198379};
RN   [1] {ECO:0000313|EMBL:SNR40112.1, ECO:0000313|Proteomes:UP000198379}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25597 {ECO:0000313|EMBL:SNR40112.1,
RC   ECO:0000313|Proteomes:UP000198379};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) 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   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. Csd subfamily.
CC       {ECO:0000256|ARBA:ARBA00010447}.
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DR   EMBL; FZNY01000001; SNR40112.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A238W0N8; -.
DR   OrthoDB; 9804366at2; -.
DR   Proteomes; UP000198379; Unassembled WGS sequence.
DR   GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006534; P:cysteine metabolic process; IEA:InterPro.
DR   CDD; cd06453; SufS_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; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR010970; Cys_dSase_SufS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR01979; sufS; 1.
DR   PANTHER; PTHR43586; CYSTEINE DESULFURASE; 1.
DR   PANTHER; PTHR43586:SF27; CYSTEINE DESULFURASE 1, CHLOROPLASTIC; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:SNR40112.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198379}.
FT   DOMAIN          32..400
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   412 AA;  44781 MW;  4EC8C8B462CB13B3 CRC64;
     MAATTSHTNF DVQNIRKDFP ILSRKVNGQP LIYFDNAATS QTPQAVIDAI VDYYSNYNAN
     IHRGVHALSQ EATDAYEEAR IKIQKHFNAA KSYEIILTAG TTHAINLIAN GYSALLQKGD
     EVLVSALEHH SNIVPWQMLC ERTGAILKVI PMTQSGELDM DAFAKAVSDK LKLVFVNHVS
     NALGTVNPIE HIIAEAHKVG AAVVIDGAQA TPHIKPDVQA LDADFYVASA HKICGPTGVG
     ILYGKEALLE KLPPYQGGGE MIDQVTFEKT TYAGLPHKFE AGTPNICGGI ATGVGLDYMN
     AIGFDVIAAY EEELLQYATE KLLKIEGLKI YGESSKKTAV VSFNVGAIHP YDIGTILDKL
     GIAVRTGHHC AQPIMDYFKI PGTVRASFSF YNTKEEIDIF IKGVERAVMM LS
//
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