ID A0A1S8W6F8_9FUNG Unreviewed; 740 AA.
AC A0A1S8W6F8;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN ORFNames=BSLG_01032 {ECO:0000313|EMBL:OON10066.1};
OS Batrachochytrium salamandrivorans.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Chytridiomycetes; Rhizophydiales;
OC Rhizophydiales incertae sedis; Batrachochytrium.
OX NCBI_TaxID=1357716 {ECO:0000313|EMBL:OON10066.1, ECO:0000313|Proteomes:UP000189906};
RN [1] {ECO:0000313|EMBL:OON10066.1, ECO:0000313|Proteomes:UP000189906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BS {ECO:0000313|EMBL:OON10066.1,
RC ECO:0000313|Proteomes:UP000189906};
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-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:OON10066.1}.
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DR EMBL; LYON01000089; OON10066.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S8W6F8; -.
DR STRING; 1357716.A0A1S8W6F8; -.
DR VEuPathDB; FungiDB:BSLG_01032; -.
DR OrthoDB; 212394at2759; -.
DR Proteomes; UP000189906; 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 GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0044571; P:[2Fe-2S] cluster assembly; IEA:InterPro.
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 HAMAP; MF_00331; Cys_desulf_IscS; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR InterPro; IPR010240; Cys_deSase_IscS.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000189906}.
FT DOMAIN 165..521
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 740 AA; 80955 MW; 6C32969175A66BD5 CRC64;
MRQTALARLT ALTGPAEQFR GAQSLFRTAG SSVWASRNSS AVYSCASVTA FGLARKSAYF
STTFMPATRS TVHCHATSSH LFHTSTKAAV IAAINSDSSA AESGSSTVIS SFSDAAKTSA
DPVKADTKDS PSSLLATAAA VRPIYLDLQA RLLPSNRIFL LDLLAATTPM DPRVLDKMMP
YMTHMYGNPH SRTHQYGWES EAAVEAGREE IANLVGADPK EIIFTSGATE SNNLAIKGVA
RFYKSKKRHI ITTQTEHKCV LDSCRVLSEE GFDVTFLPVM SNGLVDLKVL EAAIRPDTSI
VSVMTVNNEI GVIQPIKEIG RICREHKVFF HTDAAQAVGK IPIDVNDMNI DLMSISGHKI
YGPKGIGALY VRRRPRVRLE PLISGGGQER GLRSGTVPTP LVVGFGEACR LAKAEMETDG
VRIKKLSDRL IKTLTEKVRD VVRNGAPESS YPGCVNLSFA YVEGESLLMA LKAIALSSGS
ACTSASLEPS YVLRALGADD ETAHSSIRFG IGRFTTDEEV DFAINEVLQH VERLREMSPL
WEMVRYFGRN GGAMFKKVLT SNPLIGRNIS HGLHEHAVII TTNIKRSRDI YMVCLELFID
EQPRYNANLI LVFDQSRAHG TRYLMLARMD ALWTARKAIQ IGILVDTHPF SVDHCILCNQ
QLLSTSIAHL VVECEQVTDH RIQSGLVPAI QKSRLRLLGR ALDPGVEDVY TWLRGGVLNE
RSRSGPALAK LTCSTNPFYA
//