ID   NIFS_LACDA              Reviewed;         385 AA.
AC   P31672; Q1GAV2;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 2.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=NifS/IcsS protein homolog {ECO:0000305};
GN   OrderedLocusNames=Ldb0724;
OS   Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081
OS   / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB 11778 / NCTC 12712 / WDCM
OS   00102 / Lb 14).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=390333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11842 / DSM 20081 / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB
RC   11778 / NCTC 12712 / WDCM 00102 / Lb 14;
RX   PubMed=16754859; DOI=10.1073/pnas.0603024103;
RA   van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K., Nicolas P.,
RA   Robert C., Oztas S., Mangenot S., Couloux A., Loux V., Dervyn R., Bossy R.,
RA   Bolotin A., Batto J.-M., Walunas T., Gibrat J.-F., Bessieres P.,
RA   Weissenbach J., Ehrlich S.D., Maguin E.;
RT   "The complete genome sequence of Lactobacillus bulgaricus reveals extensive
RT   and ongoing reductive evolution.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 12-366.
RX   PubMed=8031904; DOI=10.1016/0300-9084(94)90061-2;
RA   Leong-Morgenthaler P.M., Oliver S., Soell D.;
RT   "A Lactobacillus nifS-like gene suppresses an Escherichia coli transaminase
RT   B mutation.";
RL   Biochimie 76:45-49(1994).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:P05341};
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. NifS/IscS subfamily. {ECO:0000305}.
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DR   EMBL; CR954253; CAI97551.1; -; Genomic_DNA.
DR   EMBL; X61190; CAA43493.1; -; Genomic_DNA.
DR   PIR; S16047; S16047.
DR   RefSeq; WP_003623519.1; NZ_JQAV01000001.1.
DR   AlphaFoldDB; P31672; -.
DR   SMR; P31672; -.
DR   STRING; 390333.Ldb0724; -.
DR   EnsemblBacteria; CAI97551; CAI97551; Ldb0724.
DR   KEGG; ldb:Ldb0724; -.
DR   PATRIC; fig|390333.13.peg.77; -.
DR   eggNOG; COG1104; Bacteria.
DR   HOGENOM; CLU_003433_0_0_9; -.
DR   OMA; APHIINF; -.
DR   BioCyc; LDEL390333:LDB_RS03160-MON; -.
DR   Proteomes; UP000001259; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
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   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF005572; NifS; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   3: Inferred from homology;
KW   Iron; Iron-sulfur; Metal-binding; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..385
FT                   /note="NifS/IcsS protein homolog"
FT                   /id="PRO_0000150290"
FT   ACT_SITE        325
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P05341"
FT   BINDING         69..70
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT   BINDING         149
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:O29689"
FT   BINDING         178
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT   BINDING         199..201
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT   BINDING         237
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT   BINDING         325
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_note="ligand shared with IscU"
FT                   /note="via persulfide group"
FT                   /evidence="ECO:0000250|UniProtKB:O29689"
FT   MOD_RES         202
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6B9"
SQ   SEQUENCE   385 AA;  42291 MW;  550234A48DEB48CE CRC64;
     MIYFDNSATT KMAPKALETY SQVVTKIWGN PSSLHKLGDR AHGLLEASRK QVADLLGVNT
     DEIYFTSGGT ESNNTAIKGT AWAKREFGKH IITSSVEHAS VANTFTELEN LGFRVTRLPV
     DKEGRVNPED LKAALDKDTT LVSIMGVNNE IGTIQPIKEI SEILADYPNI HFHVDNVQAL
     GKGIWDQVFT SRVDMMSFSS HKFHGPRGIG ILYKKRGRML MPLCEGGGQE KGLRSGTENL
     AAIAAMAKAA RLLLTDEKEK ADREYAIKEK ISKYLAGKPG IHIFSPLKAD FAPHILCFAL
     EGIRGETLVH TLEDQDIYIS TTSACASKKA DEASTLVAMK TPDAIATSAV RLSFDESNTL
     EEADEFIAAF DEIYQHFSKI NHLGE