NIFS2_TRIV2
ID NIFS2_TRIV2 Reviewed; 398 AA.
AC Q44482; Q3M592;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Cysteine desulfurase 2 {ECO:0000250|UniProtKB:P05341};
DE EC=2.8.1.7 {ECO:0000250|UniProtKB:P05341};
DE AltName: Full=Nitrogenase metalloclusters biosynthesis protein nifS2 {ECO:0000250|UniProtKB:P05341};
GN Name=nifS2 {ECO:0000250|UniProtKB:P05341}; OrderedLocusNames=Ava_4245;
OS Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX NCBI_TaxID=240292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=7568132; DOI=10.1073/pnas.92.20.9358;
RA Thiel T., Lyons E.M., Erker J.C., Ernst A.;
RT "A second nitrogenase in vegetative cells of a heterocyst-forming
RT cyanobacterium.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:9358-9362(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29413 / PCC 7937;
RX PubMed=25197444; DOI=10.4056/sigs.3899418;
RA Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL Stand. Genomic Sci. 9:562-573(2014).
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:0000269|PubMed:7568132}.
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 -!- MISCELLANEOUS: Belongs to NIF2 gene cluster which is expressed in
CC vegetative cells and heterocysts under anaerobic conditions only. This
CC second system appears to serve as an auxiliary system that does not
CC suppress expression of the first system. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. NifS/IscS subfamily. {ECO:0000305}.
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DR EMBL; U49859; AAA93018.1; -; Genomic_DNA.
DR EMBL; CP000117; ABA23844.1; -; Genomic_DNA.
DR AlphaFoldDB; Q44482; -.
DR SMR; Q44482; -.
DR STRING; 240292.Ava_4245; -.
DR EnsemblBacteria; ABA23844; ABA23844; Ava_4245.
DR KEGG; ava:Ava_4245; -.
DR eggNOG; COG1104; Bacteria.
DR HOGENOM; CLU_003433_0_0_3; -.
DR Proteomes; UP000002533; 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 Transferase.
FT CHAIN 1..398
FT /note="Cysteine desulfurase 2"
FT /id="PRO_0000150249"
FT ACT_SITE 323
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 323
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 291..293
FT /note="SNT -> PTP (in Ref. 1; AAA93018)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 398 AA; 42955 MW; 31AF52AFC41858C8 CRC64;
MSVIYLDNNA TTQVDAEVLA AMLPYLTEFY GNPSSMHTFG GQVGKAVQQA RGQVAFLLGA
EESEIIFTSC GTEGNNAAIK AALAAQPEKR HIITTQVEHA AIINVCKQLE KQGYKVTYLS
VDSQGQIDLL ELEAALTGDT ALVSTMYANN ETGVVFPIEQ IGLRAKDAGA IFHVDAVQAV
GKVPLNLKTS SIDMLTLSGH KLHAPKGIGA LYIRRGVRFR PLLVGGHQER GRRAGTENVP
GMIALGKAAE LAQIHLKDVK REKALRDRLE QGLLSAIPNT EVNGHPTSRL SNTTNIGFKY
IEGEAILLSL NKYGICASSG SACTSGSLES SHVLRAMGLP YTILHGSIRF SLSRYTTEAE
IDKVLQLMPP IVERLRAISP FSNDQADWLQ GREEALAH
