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Database: UniProt
Entry: A0A1M3QZX9_9SPHI
LinkDB: A0A1M3QZX9_9SPHI
Original site: A0A1M3QZX9_9SPHI 
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}.
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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
//
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