NIFS_BACSU
ID NIFS_BACSU Reviewed; 395 AA.
AC P38033;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Putative cysteine desulfurase NifS {ECO:0000305};
DE EC=2.8.1.7 {ECO:0000250|UniProtKB:P05341};
GN Name=nifS; Synonyms=iscS; OrderedLocusNames=BSU27880;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=168;
RX PubMed=8444804; DOI=10.1128/jb.175.5.1423-1432.1993;
RA Sun D., Setlow P.L.;
RT "Cloning, nucleotide sequence, and regulation of the Bacillus subtilis nadB
RT gene and a nifS-like gene, both of which are essential for NAD
RT biosynthesis.";
RL J. Bacteriol. 175:1423-1432(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
CC -!- FUNCTION: Catalyzes the removal of elemental sulfur from cysteine to
CC produce alanine (By similarity). Seems to be required for NAD
CC biosynthesis (PubMed:8444804). {ECO:0000250|UniProtKB:P05341,
CC ECO:0000269|PubMed:8444804}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-
CC alanine; Xref=Rhea:RHEA:43892, Rhea:RHEA-COMP:14737, Rhea:RHEA-
CC COMP:14739, ChEBI:CHEBI:29917, ChEBI:CHEBI:35235, ChEBI:CHEBI:57972,
CC ChEBI:CHEBI:64428; EC=2.8.1.7;
CC Evidence={ECO:0000250|UniProtKB:P05341};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P05341};
CC -!- INDUCTION: Repressed in the presence of nicotinic acid.
CC {ECO:0000269|PubMed:8444804}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene require nicotinic acid
CC for growth. {ECO:0000269|PubMed:8444804}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. NifS/IscS subfamily. {ECO:0000305}.
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DR EMBL; M98822; AAA21613.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14748.1; -; Genomic_DNA.
DR PIR; B47071; B47071.
DR RefSeq; NP_390666.1; NC_000964.3.
DR RefSeq; WP_004398844.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P38033; -.
DR SMR; P38033; -.
DR STRING; 224308.BSU27880; -.
DR jPOST; P38033; -.
DR PaxDb; P38033; -.
DR PRIDE; P38033; -.
DR EnsemblBacteria; CAB14748; CAB14748; BSU_27880.
DR GeneID; 936637; -.
DR KEGG; bsu:BSU27880; -.
DR PATRIC; fig|224308.179.peg.3029; -.
DR eggNOG; COG1104; Bacteria.
DR InParanoid; P38033; -.
DR OMA; CLQSANH; -.
DR PhylomeDB; P38033; -.
DR BioCyc; BSUB:BSU27880-MON; -.
DR Proteomes; UP000001570; 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; 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 2: Evidence at transcript level;
KW Iron; Iron-sulfur; Metal-binding; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..395
FT /note="Putative cysteine desulfurase NifS"
FT /id="PRO_0000150286"
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 177
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT BINDING 197..199
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT BINDING 235
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 /note="via persulfide group"
FT /evidence="ECO:0000250|UniProtKB:O29689"
FT MOD_RES 200
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
SQ SEQUENCE 395 AA; 43786 MW; 36B15B9DC35507DA CRC64;
MIYLDYAATT PICEEALTVY QKLSMDMYGN ASSLHDAGGK AKHILEYCRE KIANIIGGEA
SGIYFTSGGT ESNFLAIQSL LNGLPKTKRH FITTAMEHQS IHNCAAFLEQ QGYDVTVIEP
NEYGLITEEI LLTHIRPETG LVSIQHANSE TGIIQPIQHL SSYLHNKGIL LHCDAVQTFG
KIPINTKNLG VDALSMSSHK IHGPKGVGAV YIRPDVPWKP VYPLTTHEYG FRAGTVNVPG
IGAFTAAAEL IVSEMEKQIS RNEALRTYFL DQIRIRSLPV TLAADTSKAE CLPHIIGCFF
HSFEGQYVML ECNRSNICIS TGSACSAGYH GPSETMKALR KTEQEALQFI RISFGRHTTA
EQLEQLLHTF TVLWEQKKGE FDIDRRIKAN GRQQA
