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Database: UniProt
Entry: A0A0C2B7U2_9ACTN
LinkDB: A0A0C2B7U2_9ACTN
Original site: A0A0C2B7U2_9ACTN 
ID   A0A0C2B7U2_9ACTN        Unreviewed;       463 AA.
AC   A0A0C2B7U2;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   25-OCT-2017, entry version 18.
DE   SubName: Full=Cysteine desulfurase {ECO:0000313|EMBL:KIF74116.1};
GN   ORFNames=QR77_09170 {ECO:0000313|EMBL:KIF74116.1};
OS   Streptomyces sp. 150FB.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1576605 {ECO:0000313|EMBL:KIF74116.1, ECO:0000313|Proteomes:UP000031584};
RN   [1] {ECO:0000313|EMBL:KIF74116.1, ECO:0000313|Proteomes:UP000031584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=150FB {ECO:0000313|EMBL:KIF74116.1,
RC   ECO:0000313|Proteomes:UP000031584};
RA   Tarkka M.T., Feldhahn L., Kruger D., Buscot F., Wubet T.;
RT   "Genome sequence of the mycoparasite antagonist Streptomyces sp.
RT   strain FB 150.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|SAAS:SAAS00639066};
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|SAAS:SAAS00639095}.
CC   -!- SIMILARITY: Belongs to the sulfur carrier protein TusA family.
CC       {ECO:0000256|SAAS:SAAS00784432}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KIF74116.1}.
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DR   EMBL; JTHL01000001; KIF74116.1; -; Genomic_DNA.
DR   RefSeq; WP_040020862.1; NZ_JTHL01000001.1.
DR   EnsemblBacteria; KIF74116; KIF74116; QR77_09170.
DR   Proteomes; UP000031584; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   Gene3D; 3.30.110.40; -; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 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_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
DR   InterPro; IPR001455; TusA-like.
DR   InterPro; IPR036868; TusA-like_sf.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   Pfam; PF01206; TusA; 1.
DR   PIRSF; PIRSF005572; NifS; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   SUPFAM; SSF64307; SSF64307; 1.
DR   PROSITE; PS01148; UPF0033; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000031584};
KW   Pyridoxal phosphate {ECO:0000256|SAAS:SAAS00639089};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031584}.
FT   DOMAIN      394    418       UPF0033. {ECO:0000259|PROSITE:PS01148}.
SQ   SEQUENCE   463 AA;  48169 MW;  7E74747F529FB8C1 CRC64;
     MPYFDAASSA PLHPVAREAL QASLDEGWAD PARLYREGRR ARMLLDAARE AAAEAVGCRP
     DELVFTPSGT AAVHSAMAGA LFARRRVGTH AVVSAVEHSS VLHAAHTHAE ATGGAVTEVP
     VDRYGAVSPG TYARALRADT ALAVLQSANH EVGTEQPVAE VAGTCRERGV PLLVDAAQSL
     GWGPLDADWS LLAASAHKWG GPGGVGLLAV RKGVRFAPQG PADERESGRA PGFENIPAVV
     AAAASLRAVR AEAADEAARL RALVDRIRAR VPELVPDVEV VGDPVRRLPH LVTFSCLYVD
     GEALLHELDR ADFSVNSGSS CTSSTLTPSH VLRAMGVLSE GNVRVSLPRG TTEAEVDRFL
     AVLPGAVSGV RERLGVPAAA LSAPAAGGPA SLTVDALGRR CPIPVIELAK VIGDVPVGGT
     VTVLADDEAA RLDIPAWCEM RGQEYLGEEP ADHGAAYVVR RAS
//
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