ID A0A5M9WIK3_9LACO Unreviewed; 410 AA. AC A0A5M9WIK3; A0A6P1TWJ6; DT 26-FEB-2020, integrated into UniProtKB/TrEMBL. DT 26-FEB-2020, sequence version 1. DT 13-SEP-2023, entry version 12. DE RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239}; DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239}; GN Name=sufS {ECO:0000313|EMBL:QHQ67934.1}; GN ORFNames=GSR61_04840 {ECO:0000313|EMBL:QHQ67934.1}; OS Lactobacillus crispatus. OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=47770 {ECO:0000313|EMBL:QHQ67934.1, ECO:0000313|Proteomes:UP000464915}; RN [1] {ECO:0000313|EMBL:QHQ67934.1, ECO:0000313|Proteomes:UP000464915} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C25 {ECO:0000313|EMBL:QHQ67934.1, RC ECO:0000313|Proteomes:UP000464915}; RA Hassan H.M., Mendoza M., Rezvani M., Koci M.D., Dickey A.N., Scholl E.H.; RT "Complete Genome Sequences of Lactobacillus strains, C25 and P38, Isolated RT from Chicken Cecum."; RL Submitted (DEC-2019) 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP047142; QHQ67934.1; -; Genomic_DNA. DR RefSeq; WP_065990616.1; NZ_VYYV01000001.1. DR AlphaFoldDB; A0A5M9WIK3; -. DR Proteomes; UP000464915; Chromosome. DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC. 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; 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:SF8; CYSTEINE DESULFURASE 1, CHLOROPLASTIC; 1. DR Pfam; PF00266; Aminotran_5; 1. DR PIRSF; PIRSF005572; NifS; 1. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. PE 3: Inferred from homology; FT DOMAIN 27..395 FT /note="Aminotransferase class V" FT /evidence="ECO:0000259|Pfam:PF00266" SQ SEQUENCE 410 AA; 45742 MW; 4BDAB11010393FC2 CRC64; MDKEAITKIR NDFPILKQKI NGNRLAYLDN AATMQMPVPI LHKINSFYQT SYANVHRSVD TLGFNATKQY EEARGKVASF INAADANEII FTSGCTDSLN LVAATYGEQN IHEQDEIVLT IMEHHSNLLP WQQLAKRKGA ILKYIDLTES QTLDLDDVKK KITAKTKIVA IAHASNILGM MNPIEEVIKI AHQVEAVVVV DGAQAVSHFP IDVQKLDADF YAFSGHKMLA PTGIGVLYGK KNLLNQMPPY RFGGEMIGNV TKYNATWADL PQKFEAGTPN IIGAIGLGYA IDYLHEIGMN RIQTYENELS KYLMQKIEKL DFVAIYGPKE NHTGVFSFNL KNIHPHDVAT ALDMQGIEVR AGHHCAQPLM RRLGVESTVR ASLSFYNNKE DIDQLIAGIS ETEEFFNGTK //