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Database: UniProt
Entry: A0A150J7I5_9EURY
LinkDB: A0A150J7I5_9EURY
Original site: A0A150J7I5_9EURY 
ID   A0A150J7I5_9EURY        Unreviewed;       388 AA.
AC   A0A150J7I5;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Putative cysteine desulfurase 2 {ECO:0000313|EMBL:KYC53151.1};
DE            EC=2.8.1.7 {ECO:0000313|EMBL:KYC53151.1};
GN   Name=iscS2 {ECO:0000313|EMBL:KYC53151.1};
GN   ORFNames=AMQ74_00483 {ECO:0000313|EMBL:KYC53151.1};
OS   Candidatus Methanofastidiosum methylthiophilus.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Candidatus Methanofastidiosa;
OC   Methanofastidiosum.
OX   NCBI_TaxID=1705564 {ECO:0000313|EMBL:KYC53151.1, ECO:0000313|Proteomes:UP000075578};
RN   [1] {ECO:0000313|EMBL:KYC53151.1, ECO:0000313|Proteomes:UP000075578}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U1lsi0528_Bin089 {ECO:0000313|EMBL:KYC53151.1};
RX   PubMed=26943620;
RA   Nobu M.K., Narihiro T., Kuroda K., Mei R., Liu W.T.;
RT   "Chasing the elusive Euryarchaeota class WSA2: genomes reveal a uniquely
RT   fastidious methyl-reducing methanogen.";
RL   ISME J. 0:0-0(2016).
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. 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:KYC53151.1}.
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DR   EMBL; LNGD01000017; KYC53151.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A150J7I5; -.
DR   PATRIC; fig|1705564.3.peg.490; -.
DR   Proteomes; UP000075578; 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; 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; 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.
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};
KW   Transferase {ECO:0000313|EMBL:KYC53151.1}.
FT   DOMAIN          5..366
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   388 AA;  43194 MW;  3821317253A165EC CRC64;
     MEKNVYLDNA AATRLDERVL EAMKKYFFEV YAVATSEFGY SLGIEAREAL EEARGVIANK
     LGAEHDEIVF TSGSTESSNM AIKGVALALK EKKGKHIIVS KIEDFPVLNS AKSLEKQGFE
     ITYLDVDQHG LVNFEQLENS IRNDTILVSI QHANQEIGTL QDINRIGNLC KQKGVLFHTD
     ATHTFTRIPI DVKKIHANLI TVSAHTIHGP KETGALFIRK NTPLTKWMDG GFQEFNKRAG
     LENIPGAVGF AKAVELVTQE ENNKLQQFRD YLIKRVLTEI PNTTLNGHLE KRIPHNANIT
     FHYVEGESIT LHLDMRGFSV STGSACFSKS LEASHVIMGI GGDHERAHGS VRFTFGRYNT
     MEDVNSVVDN ISEVVEELRK ISPLGKNS
//
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