NIFS_KLEPN
ID NIFS_KLEPN Reviewed; 397 AA.
AC P05344;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 2.
DT 03-AUG-2022, entry version 99.
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};
OS Klebsiella pneumoniae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3054814; DOI=10.1093/nar/16.20.9860;
RA Beynon J., Cannon M., Banan-Wollaston V., Ally A., Sutterquist R.,
RA Cannon F.;
RT "The nucleotide sequence of the nifT, nifY, nifX and nifW genes of K.
RT pneumoniae.";
RL Nucleic Acids Res. 16:9860-9860(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3040672; DOI=10.1128/jb.169.9.4024-4029.1987;
RA Beynon J., Ally A., Cannon M., Cannon F., Jacobson M.R., Cash V.L.,
RA Dean D.R.;
RT "Comparative organization of nitrogen fixation-specific genes from
RT Azotobacter vinelandii and Klebsiella pneumoniae: DNA sequence of the
RT nifUSV genes.";
RL J. Bacteriol. 169:4024-4029(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3062178; DOI=10.1016/0022-2836(88)90205-7;
RA Arnold W., Rump A., Klipp W., Priefer U.B., Puehler A.;
RT "Nucleotide sequence of a 24,206-base-pair DNA fragment carrying the entire
RT nitrogen fixation gene cluster of Klebsiella pneumoniae.";
RL J. Mol. Biol. 203:715-738(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; X12600; CAA31118.1; -; Genomic_DNA.
DR EMBL; M17350; AAA25156.1; -; Genomic_DNA.
DR EMBL; X13303; CAA31675.1; -; Genomic_DNA.
DR PIR; S02507; S02507.
DR AlphaFoldDB; P05344; -.
DR SMR; P05344; -.
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 Transferase.
FT CHAIN 1..397
FT /note="Cysteine desulfurase"
FT /id="PRO_0000150256"
FT ACT_SITE 321
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000250|UniProtKB:P05341"
FT BINDING 148
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:O29689"
FT BINDING 176
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT BINDING 196..198
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT BINDING 234
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT BINDING 321
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 199
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT CONFLICT 71..79
FT /note="WPRATPRHA -> CATEATATAIAS (in Ref. 3; CAA31675)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="L -> M (in Ref. 3; CAA31675)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="Q -> E (in Ref. 3; CAA31675)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="S -> G (in Ref. 3; CAA31675)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="D -> H (in Ref. 2; AAA25156)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="G -> P (in Ref. 2; AAA25156)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="R -> A (in Ref. 3; CAA31675)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 397 AA; 43254 MW; EE81BE82D0F21F48 CRC64;
MKQVYLDNNA TTRLDPMVLE AMMPFLTDFY GNPSSIHDFG IPAQAALERA HQQAAALLGA
EYPSEIIFTS WPRATPRHAA IALLPERREI ITSVVEHPAT LAACEHLERQ GYRIHRIAVD
SEGALDMAQF RAALSPRVAL VSVMWANNET GVLFPIGEMA ELAHEQGALF HCDAVQVVGK
IPIAVGQTRI DMLSCSAHKF HGPKGVGCLY LRRGTRFRPL LRGGHQEYGR RAGTENICGI
VGMGAACELA NIHLPGMTHI GQLRNRLEHR LLASVPSVMV MGGGQPRVPG TVNLAFEFIE
GEAILLLLNQ AGIAASSGSA CTSGSLEPSH VMRAMNIPYT AAHGTIRFSL SRYTREKEID
YVVATLPPII DRLRALSPYW QNGKPRPADA VFTPVYG
