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Database: UniProt
Entry: G1UB03_LACJO
LinkDB: G1UB03_LACJO
Original site: G1UB03_LACJO 
ID   G1UB03_LACJO            Unreviewed;       384 AA.
AC   G1UB03;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   SubName: Full=Cysteine desulfurase NifS {ECO:0000313|EMBL:AAS08806.1};
GN   OrderedLocusNames=LJ_0984 {ECO:0000313|EMBL:AAS08806.1};
OS   Lactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=257314 {ECO:0000313|EMBL:AAS08806.1, ECO:0000313|Proteomes:UP000000581};
RN   [1] {ECO:0000313|EMBL:AAS08806.1, ECO:0000313|Proteomes:UP000000581}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNCM I-1225 / La1 / NCC 533
RC   {ECO:0000313|Proteomes:UP000000581};
RX   PubMed=14983040; DOI=10.1073/pnas.0307327101;
RA   Pridmore R.D., Berger B., Desiere F., Vilanova D., Barretto C.,
RA   Pittet A.-C., Zwahlen M.-C., Rouvet M., Altermann E., Barrangou R.,
RA   Mollet B., Mercenier A., Klaenhammer T., Arigoni F., Schell M.A.;
RT   "The genome sequence of the probiotic intestinal bacterium Lactobacillus
RT   johnsonii NCC 533.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:2512-2517(2004).
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}.
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DR   EMBL; AE017198; AAS08806.1; -; Genomic_DNA.
DR   RefSeq; WP_011161850.1; NC_005362.1.
DR   AlphaFoldDB; G1UB03; -.
DR   GeneID; 83570579; -.
DR   KEGG; ljo:LJ_0984; -.
DR   PATRIC; fig|257314.6.peg.844; -.
DR   eggNOG; COG1104; Bacteria.
DR   HOGENOM; CLU_003433_0_0_9; -.
DR   Proteomes; UP000000581; Chromosome.
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; IPR018247; EF_Hand_1_Ca_BS.
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; PS00018; EF_HAND_1; 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..371
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   384 AA;  42520 MW;  47DD020454D5024F CRC64;
     MTRKNVYLDN AATTPMDPKV IEKISSEMAD DFGNASSQHA FGRKARHVVE TARHQLAETI
     NAQDKEIIFT SGGSESNNTA IFGTVRARKD IGKKIITTKI EHPSVLNPMK RLAQEGYEIV
     YLDVDETGHI NLDDLKRELT PDTILVSIMA VNNEVGSIMP LKEIGELVKD SNAYFHVDDV
     QGFGNIEIDV KEMNIDLLST SAHKVNGPKF LGFLYEKNGL KVSNLLLGGE QETKRRPGTE
     NVPGIAGFGI AAQELNEMDK QKLQEKYQNF QKIILDELDK NQIDYEVNGT LEGKVSHHVL
     NLWLKGVGTY SALTNLDLSG YAVSGGSACT AGSLTPSHVL QAMYGEDSPR IEESIRISFG
     RFNTEEEIQE FAADLVKMCK RLDK
//
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