FIXZ_RHILE
ID FIXZ_RHILE Reviewed; 465 AA.
AC P07748;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2017, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=FeMo cofactor biosynthesis protein FixZ;
DE EC=4.-.-.-;
DE AltName: Full=Nitrogen fixation protein FixZ;
DE Flags: Fragment;
GN Name=fixZ;
OS Rhizobium leguminosarum.
OG Plasmid sym pRL1JI.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=384;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6091056; DOI=10.1093/nar/12.18.7123;
RA Rossen L., Ma Q.-S., Mudd E.A., Johnston A.W.B., Downie J.A.;
RT "Identification and DNA sequence of fixZ, a nifB-like gene from Rhizobium
RT leguminosarum.";
RL Nucleic Acids Res. 12:7123-7134(1984).
CC -!- FUNCTION: Involved in the biosynthesis of the iron-molybdenum cofactor
CC (FeMo-co or M-cluster) found in the dinitrogenase enzyme of the
CC nitrogenase complex in nitrogen-fixing microorganisms. Catalyzes the
CC crucial step of radical SAM-dependent carbide insertion that occurs
CC concomitant with the insertion of a 9th sulfur and the
CC rearrangement/coupling of two [4Fe-4S] clusters into a [8Fe-9S-C]
CC cluster, the precursor to the M-cluster.
CC {ECO:0000250|UniProtKB:D5VRM1}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:D5VRM1};
CC Note=Binds 3 [4Fe-4S] clusters per monomer. One cluster is coordinated
CC with 3 cysteines and an exchangeable S-adenosyl-L-methionine. The two
CC others probably act as substrate. {ECO:0000250|UniProtKB:D5VRM1};
CC -!- PATHWAY: Cofactor biosynthesis; Fe-Mo cofactor biosynthesis.
CC {ECO:0000250|UniProtKB:D5VRM1}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. NifB family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA25481.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X00976; CAA25481.1; ALT_FRAME; Genomic_DNA.
DR PIR; A22891; A22891.
DR UniPathway; UPA00782; -.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.30.420.130; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR003731; Di-Nase_FeMo-co_biosynth.
DR InterPro; IPR036105; DiNase_FeMo-co_biosyn_sf.
DR InterPro; IPR000385; MoaA_NifB_PqqE_Fe-S-bd_CS.
DR InterPro; IPR005980; Nase_CF_NifB.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR43787:SF3; PTHR43787:SF3; 1.
DR Pfam; PF02579; Nitro_FeMo-Co; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SUPFAM; SSF53146; SSF53146; 1.
DR TIGRFAMs; TIGR01290; nifB; 1.
DR PROSITE; PS01305; MOAA_NIFB_PQQE; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding; Nitrogen fixation;
KW Plasmid; S-adenosyl-L-methionine.
FT CHAIN 1..>465
FT /note="FeMo cofactor biosynthesis protein FixZ"
FT /id="PRO_0000153042"
FT DOMAIN 61..312
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT REGION 17..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 75
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:P69848"
FT BINDING 79
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:P69848"
FT BINDING 81
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P69848"
FT BINDING 82
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:P69848"
FT BINDING 129
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P69848"
FT BINDING 181
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P69848"
FT BINDING 233
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P69848"
FT BINDING 306
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:D5VRM1"
FT BINDING 309
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:D5VRM1"
FT NON_TER 465
SQ SEQUENCE 465 AA; 50942 MW; 3765BACA3C024A54 CRC64;
MSEPEIKVGK TSSALFDRAP MAPSMPGGRA SSSHGLSVTD DIDARIWERI KDHPCFSEXA
HHYFARMHXX VAPACNIQCN YCNRKYDCTN ESCPXVASVK LTPDQALRKV LAVASKVPEL
SVIXVAGPGD ACYDWRKTVA TFEGVAREIP DMKLCISTNG LALPDHVDEL ADMNIDHVTI
TINMVDPEIG AKIYPWIIHG HRRYTGIAAA GILHERQMLG LELLTKRGIL TKINSVMIPG
VNDTHLVEVN RWIRDRGAFM HNVVPLISKP SHGTYYGLTG QRCPEPFELK ALQDCLDGNI
KLMRHCQQCR ADAIGLLGDD REREFALDQI STKVEFDTSK REAYRKLVQH ERGDQLAAKL
DANKAVKSLG SSGTLAVAVA TKGGGRINEH FGQARELQVY AVSLKGINLV GHXXVEQYCL
GGIGEKATLD HTIVALDGID ILLSSKIGDC PKKRLAETGV RASDA
