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Database: UniProt
Entry: G7CEP0_MYCT3
LinkDB: G7CEP0_MYCT3
Original site: G7CEP0_MYCT3 
ID   G7CEP0_MYCT3            Unreviewed;       398 AA.
AC   G7CEP0;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=Cysteine desulfurase {ECO:0000313|EMBL:EHI13582.1};
GN   ORFNames=KEK_07282 {ECO:0000313|EMBL:EHI13582.1};
OS   Mycolicibacterium thermoresistibile (strain ATCC 19527 / DSM 44167 / CIP
OS   105390 / JCM 6362 / NCTC 10409 / 316) (Mycobacterium thermoresistibile).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1078020 {ECO:0000313|EMBL:EHI13582.1, ECO:0000313|Proteomes:UP000004915};
RN   [1] {ECO:0000313|EMBL:EHI13582.1, ECO:0000313|Proteomes:UP000004915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19527 / DSM 44167 / CIP 105390 / JCM 6362 / NCTC 10409 /
RC   316 {ECO:0000313|Proteomes:UP000004915};
RG   Tuberculosis Structural Genomics Consortium;
RA   Ioerger T.R.;
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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:EHI13582.1}.
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DR   EMBL; AGVE01000040; EHI13582.1; -; Genomic_DNA.
DR   RefSeq; WP_003924956.1; NZ_AGVE01000040.1.
DR   AlphaFoldDB; G7CEP0; -.
DR   PATRIC; fig|1078020.3.peg.1434; -.
DR   eggNOG; COG1104; Bacteria.
DR   Proteomes; UP000004915; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000004915}.
FT   DOMAIN          7..374
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   398 AA;  41241 MW;  D61814A35E1DE368 CRC64;
     MNTPQTVYLD HAATTPMYPA AITAMTDVMS TVGNASSLHS SGRVARRRME EARETLARLL
     GARPSEVVFT AGGTESDNLA VKGLYWARRA ASPGLRRIIT TRVEHHAVLD AVDWLVQHEG
     AEVTWLPVEP DGSVTPATLR EALRAHDDVA LVTLMWANNE VGTVSPIAEL AAVAAEFSVP
     MHSDAVQAVG HLPVDFSASG LSAMSISAHK FGGPTGVGAL LIRRDAECVP LLHGGGQERD
     IRSGTPHVAG VVAMAVAAEA AIENLPAVSA RIAALRDRLI DGVLTGIDDA YLNGARGADR
     LPGNAHFTFR GCEGDSLLML LDANGIECST GSACTAGVAQ PSHVLIAMGA DSASARGSLR
     LSLGHTSTEA DVDAALAVLP AAVERARQAA LASAGVDK
//
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