ID A0A023DER4_9BACI Unreviewed; 406 AA.
AC A0A023DER4;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
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 Name=sufS {ECO:0000313|EMBL:GAJ39774.1};
GN ORFNames=GCA01S_026_00200 {ECO:0000313|EMBL:GAJ39774.1};
OS Parageobacillus caldoxylosilyticus NBRC 107762.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Parageobacillus.
OX NCBI_TaxID=1220594 {ECO:0000313|EMBL:GAJ39774.1, ECO:0000313|Proteomes:UP000023561};
RN [1] {ECO:0000313|EMBL:GAJ39774.1, ECO:0000313|Proteomes:UP000023561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 107762 {ECO:0000313|EMBL:GAJ39774.1,
RC ECO:0000313|Proteomes:UP000023561};
RA Hosoyama A., Hosoyama Y., Katano-Makiyama Y., Tsuchikane K., Ohji S.,
RA Ichikawa N., Yamazoe A., Fujita N.;
RT "Whole genome shotgun sequence of Geobacillus caldoxylosilyticus NBRC
RT 107762.";
RL Submitted (APR-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}.
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:GAJ39774.1}.
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DR EMBL; BAWO01000026; GAJ39774.1; -; Genomic_DNA.
DR RefSeq; WP_042409040.1; NZ_BAWO01000026.1.
DR AlphaFoldDB; A0A023DER4; -.
DR OrthoDB; 9804366at2; -.
DR Proteomes; UP000023561; Unassembled WGS sequence.
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:UP000023561};
KW Transferase {ECO:0000256|RuleBase:RU004506}.
FT DOMAIN 23..391
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 406 AA; 44681 MW; 129BD246056AF5AE CRC64;
MNVKEIRKLF PILDQEVNGK PLVYLDNAAT SQKPLPVIEA LDQYYRQYNS NVHRGVHTLG
TKATDAYEGA REKVRRFINA KSTQEIIFTR GTTAALNIVA ASYGRANLQE GDEIVITYME
HHSNLIPWQQ AAKQTGATLK YIPLQADGTI DIKDVEATVT ANTKIVAVAH VSNVLGTINP
IKDIARIAHQ HGAVVVVDAA QSAPHMKIDV QDLDCDFLAF SGHKMCGPTG IGVLYGKRDL
LERMEPVEFG GEMIDFVELY DSTWKELPWK FEGGTPIIAG AIGLGAAIDF LEDVGLDHIA
AHEHELAQYA LERMSAIDGL TIYGPKQRGG LVTFNIDGVH PHDVATVLDA EGIAVRAGHH
CAQPLMKWLN VTATARASFY LYNTKEEIDQ LVVALQKTKE YFGHVF
//
