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Database: UniProt
Entry: A0A0G1QBD9_9BACT
LinkDB: A0A0G1QBD9_9BACT
Original site: A0A0G1QBD9_9BACT 
ID   A0A0G1QBD9_9BACT        Unreviewed;       381 AA.
AC   A0A0G1QBD9;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Cysteine desulfurase {ECO:0000313|EMBL:KKU15053.1};
GN   ORFNames=UX23_C0005G0019 {ECO:0000313|EMBL:KKU15053.1};
OS   Parcubacteria group bacterium GW2011_GWB1_45_9.
OC   Bacteria.
OX   NCBI_TaxID=1618879 {ECO:0000313|EMBL:KKU15053.1, ECO:0000313|Proteomes:UP000034512};
RN   [1] {ECO:0000313|EMBL:KKU15053.1, ECO:0000313|Proteomes:UP000034512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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:KKU15053.1}.
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DR   EMBL; LCLK01000005; KKU15053.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1QBD9; -.
DR   PATRIC; fig|1618879.3.peg.303; -.
DR   Proteomes; UP000034512; 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          6..368
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   381 AA;  42149 MW;  250AEBAEB9612267 CRC64;
     MVNKKIYLDY AATTPVDSEV KKTMLPYFSE KFGNAGSLHS FGQEATAAID GAREKIAKAI
     GAQFREIIFT GSATEANNLA LRGVLKAKSL KVKARIIVSA IEHESVLETA KDLEREGAEV
     IYLPVNREGL VDVGKLKESL NERTILVSVM YVNNEIGTVQ PVREISKLIL EFRKHSTFPL
     FHTDAAQALQ YLDCDINNLG VDLMTLSAHK IYGPKGIGVL YAKSLKLKAI ITGGGQEFGF
     RSGTENTPLI VGFGKAVELA ARDRKRAAKK ITELRDYFWK ELKKIEPKIE VNGRIAPHIL
     NIYFPYRGSQ DFLARLDLSG ISASSGSACF ARSLVPSYVI QALGYSRERA EHSVRFSFGK
     YIGKKDIDEA LKRVKIIVDN S
//
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