ID   A0A089IHS0_9BACL        Unreviewed;       408 AA.
AC   A0A089IHS0;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239, ECO:0000256|RuleBase:RU004506};
DE            EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239, ECO:0000256|RuleBase:RU004506};
GN   ORFNames=H70737_08720 {ECO:0000313|EMBL:AIQ22927.1};
OS   Paenibacillus sp. FSL H7-0737.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1536775 {ECO:0000313|EMBL:AIQ22927.1, ECO:0000313|Proteomes:UP000029519};
RN   [1] {ECO:0000313|EMBL:AIQ22927.1, ECO:0000313|Proteomes:UP000029519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL H7-0737 {ECO:0000313|EMBL:AIQ22927.1,
RC   ECO:0000313|Proteomes:UP000029519};
RA   den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT   "Comparative genomics of the Paenibacillus odorifer group.";
RL   Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the removal of elemental sulfur and selenium atoms
CC       from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to
CC       produce L-alanine. {ECO:0000256|RuleBase:RU004506}.
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         ECO:0000256|RuleBase:RU004506};
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. {ECO:0000256|ARBA:ARBA00010447,
CC       ECO:0000256|RuleBase:RU004506}.
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DR   EMBL; CP009279; AIQ22927.1; -; Genomic_DNA.
DR   RefSeq; WP_042186355.1; NZ_CP009279.1.
DR   AlphaFoldDB; A0A089IHS0; -.
DR   KEGG; paej:H70737_08720; -.
DR   eggNOG; COG0520; Bacteria.
DR   HOGENOM; CLU_003433_2_5_9; -.
DR   Proteomes; UP000029519; Chromosome.
DR   GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006534; P:cysteine metabolic process; IEA:UniProtKB-UniRule.
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; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR   InterPro; IPR010970; Cys_dSase_SufS.
DR   InterPro; IPR016454; Cysteine_dSase.
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   PIRSF; PIRSF005572; NifS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU004506};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029519};
KW   Transferase {ECO:0000256|RuleBase:RU004506}.
FT   DOMAIN          23..392
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   408 AA;  44750 MW;  E37E1A87060E76BA CRC64;
     MISNAIREQF PILNQNVNGH PLVYLDSAAT SQKPRQVIEA VKSYYEWDNA NVHRGVHTLG
     SRATDAYEGA REKLAKFINA RSTKEIIFTR GTTTALNLVA SSYGPSAVGE GDEIVITLME
     HHSNLIPWQQ LAKKTGATLK YIPLQPDGTI TLEDAEKTIT DKTKIVAIAY VSNVMGVTHP
     IKELAAIAHR NGAVIVVDGA QSTPHMKVDM QDLDCDFYAL SGHKMLAPTG IGALYGKRAL
     LEAMEPIEFG GEMIDDVGLY ESTWKELPWK FEGGTPIIAG AVGLGAAVDF LQEIGMDEIH
     SHEKQLAAYA EQRLSEIDGL TIYGPRNREV GVVTFNLGDV HPHDVATVLD AEGIAIRAGH
     HCCQPLMRWL EASSTARASF YLYNTEQDVD RLVDALIKTK EYFGYELG
//