ID A0A1M3QZX9_9SPHI Unreviewed; 376 AA.
AC A0A1M3QZX9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Cysteine desulfurase {ECO:0000313|EMBL:OJY95800.1};
GN ORFNames=BGP13_00445 {ECO:0000313|EMBL:OJY95800.1};
OS Sphingobacteriales bacterium 40-81.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX NCBI_TaxID=1895835 {ECO:0000313|EMBL:OJY95800.1, ECO:0000313|Proteomes:UP000184064};
RN [1] {ECO:0000313|EMBL:OJY95800.1, ECO:0000313|Proteomes:UP000184064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=40-81 {ECO:0000313|EMBL:OJY95800.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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. NifS/IscS subfamily.
CC {ECO:0000256|ARBA:ARBA00006490}.
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:OJY95800.1}.
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; MKWF01000019; OJY95800.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3QZX9; -.
DR STRING; 1895835.BGP13_00445; -.
DR Proteomes; UP000184064; Unassembled WGS sequence.
DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.260.50; -; 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; IPR016454; Cysteine_dSase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11601:SF34; CYSTEINE DESULFURASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11601; CYSTEINE DESULFURYLASE FAMILY MEMBER; 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 Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT DOMAIN 5..367
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 376 AA; 41275 MW; 71A22786862DD5D6 CRC64;
MEKRIYFDNA ATTALSNDVL EAMLPYMREK FGNPSSIYSY GRESRLAIEN ARKSVAKILN
AHPAEIFFTS GGTESSNTAI TASVRDLGCT RIITSAVEHH AVLHTVEYLR NRGEAELVFV
KLLPDGHIDI DNLEQLLAGS EAKTLVTLMH GNNEIGNVLD LHAVGNLCKL YGAIFHSDTV
QTVGHYPFDL RNTPVHFITG GAHKFHGPKG VGLLYINENV RIHPYIHGGS QERNMRAGTE
NLYGIVGFAK ALELATANCQ NDSAAIKSLK LYMADKLKQN IKDVSFNGDV FGKSLYTVLN
VSFPKTEKSE MLLFNLDINN ICASGGSACT SGADQGSHVI RAINNNPNKI AVRFSFSKYN
TKEEVDVVVE KLKELI
//