NIFS_NOSS1
ID NIFS_NOSS1 Reviewed; 400 AA.
AC P12623;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 3.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Cysteine desulfurase {ECO:0000250|UniProtKB:P05341};
DE EC=2.8.1.7 {ECO:0000250|UniProtKB:P05341};
DE AltName: Full=Nitrogenase metalloclusters biosynthesis protein NifS {ECO:0000250|UniProtKB:P05341};
GN Name=nifS {ECO:0000250|UniProtKB:P05341}; OrderedLocusNames=all1457;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2553733; DOI=10.1016/s0021-9258(19)47287-6;
RA Mulligan M.E., Haselkorn R.;
RT "Nitrogen fixation (nif) genes of the cyanobacterium Anabaena species
RT strain PCC 7120. The nifB-fdxN-nifS-nifU operon.";
RL J. Biol. Chem. 264:19200-19207(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
RX PubMed=2842320; DOI=10.1128/jb.170.9.4406-4410.1988;
RA Mulligan M.E., Buikema W.J., Haselkorn R.;
RT "Bacterial-type ferredoxin genes in the nitrogen fixation regions of the
RT cyanobacterium Anabaena sp. strain PCC 7120 and Rhizobium meliloti.";
RL J. Bacteriol. 170:4406-4410(1988).
CC -!- FUNCTION: Catalyzes the removal of elemental sulfur atoms from cysteine
CC to produce alanine. Seems to participate in the biosynthesis of the
CC nitrogenase metalloclusters by providing the inorganic sulfur required
CC for the Fe-S core formation. {ECO:0000250|UniProtKB:P05341}.
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 -!- SUBUNIT: Homodimer. {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; J05111; AAA22006.1; -; Genomic_DNA.
DR EMBL; BA000019; BAB73413.1; -; Genomic_DNA.
DR PIR; AE1988; AE1988.
DR PIR; C34443; C34443.
DR RefSeq; WP_010995628.1; NZ_RSCN01000040.1.
DR AlphaFoldDB; P12623; -.
DR SMR; P12623; -.
DR STRING; 103690.17130803; -.
DR EnsemblBacteria; BAB73413; BAB73413; BAB73413.
DR KEGG; ana:all1457; -.
DR eggNOG; COG1104; Bacteria.
DR OMA; ANFSFEF; -.
DR OrthoDB; 839689at2; -.
DR Proteomes; UP000002483; 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 GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR GO; GO:0009399; P:nitrogen fixation; 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; IPR017772; Cys_deSase_NifS_bac/arc.
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 TIGRFAMs; TIGR03402; FeS_nifS; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 3: Inferred from homology;
KW Iron; Iron-sulfur; Metal-binding; Nitrogen fixation; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..400
FT /note="Cysteine desulfurase"
FT /id="PRO_0000150247"
FT ACT_SITE 324
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000250|UniProtKB:P05341"
FT BINDING 71..72
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT BINDING 150
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 198..200
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT BINDING 236
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT BINDING 324
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 201
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT CONFLICT 88
FT /note="E -> A (in Ref. 1; AAA22006)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 400 AA; 43715 MW; 478FDE824C47D5D3 CRC64;
MSVIYLDNNA TTKVDPDVVE AIMPYLTDYY GNPSSMHTFG GQLGKAVRTA REQVAALLGA
DESEIVFTSC GTEGDNAAIR AALLAQPEKR HIITTQVEHP AVLNVCKQLE TQGYTVTYLS
VNSHGQLDLD ELEASLTGNT ALVTIMYANN ETGTVFPIEE IGKRVKERGA IFHVDAVQAV
GKIPLNMKTS TIDMLTISGH KIHAPKGIGA LYVRRGVRFR PLLIGGHQER GRRAGTENVP
GIVGLGKAAE LELIHIETAI KKETRLRDRL EQTLLAKIPD CEVNGDITQR LPNTTNIGFK
YIEGEAILLS LNKYGICASS GSACTSGSLE PSHVLRAMGL PYTTLHGSIR FSLCRYTTEA
QIDRVIEVMP EIVERLRALS PFKNDEAGWL QAQEQTLAHR
