BZAF_GEOMG
ID BZAF_GEOMG Reviewed; 435 AA.
AC Q39YG0;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=5-hydroxybenzimidazole synthase {ECO:0000250|UniProtKB:P61425};
DE Short=5-OHBza synthase {ECO:0000250|UniProtKB:P61425};
DE Short=HBI synthase {ECO:0000250|UniProtKB:P61425};
DE EC=4.1.99.23 {ECO:0000250|UniProtKB:P61425};
GN Name=bzaF {ECO:0000303|PubMed:26246619};
GN Synonyms=thiC-2 {ECO:0000312|EMBL:ABB30714.1}; OrderedLocusNames=Gmet_0471;
OS Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=269799;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53774 / DSM 7210 / GS-15;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Geobacter metallireducens GS-15.";
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PREDICTED FUNCTION.
RX PubMed=26246619; DOI=10.1073/pnas.1509132112;
RA Hazra A.B., Han A.W., Mehta A.P., Mok K.C., Osadchiy V., Begley T.P.,
RA Taga M.E.;
RT "Anaerobic biosynthesis of the lower ligand of vitamin B12.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:10792-10797(2015).
CC -!- FUNCTION: Catalyzes the conversion of aminoimidazole ribotide (AIR) to
CC 5-hydroxybenzimidazole (5-HBI) in a radical S-adenosyl-L-methionine
CC (SAM)-dependent reaction. Is thus involved in the anaerobic
CC biosynthesis of the benzimidazole lower axial ligand of the cobamide
CC produced by G.metallireducens. {ECO:0000250|UniProtKB:P61425,
CC ECO:0000305|PubMed:26246619}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + AH2 + S-
CC adenosyl-L-methionine = 5'-deoxyadenosine + 5-hydroxybenzimidazole +
CC A + formate + 2 H(+) + L-methionine + NH4(+) + phosphate;
CC Xref=Rhea:RHEA:53504, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:17319, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:137404, ChEBI:CHEBI:137981;
CC EC=4.1.99.23; Evidence={ECO:0000250|UniProtKB:P61425};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P61425};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated
CC with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000250|UniProtKB:Q9A6Q5};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P61425}.
CC -!- SIMILARITY: Belongs to the ThiC family. 5-hydroxybenzimidazole synthase
CC subfamily. {ECO:0000305}.
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DR EMBL; CP000148; ABB30714.1; -; Genomic_DNA.
DR RefSeq; WP_004513840.1; NC_007517.1.
DR AlphaFoldDB; Q39YG0; -.
DR SMR; Q39YG0; -.
DR STRING; 269799.Gmet_0471; -.
DR EnsemblBacteria; ABB30714; ABB30714; Gmet_0471.
DR KEGG; gme:Gmet_0471; -.
DR eggNOG; COG0422; Bacteria.
DR HOGENOM; CLU_013181_2_2_7; -.
DR OMA; PYFVFGP; -.
DR OrthoDB; 505395at2; -.
DR Proteomes; UP000007073; Chromosome.
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:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro.
DR Gene3D; 3.20.20.540; -; 1.
DR InterPro; IPR038521; ThiC/Bza_core_dom.
DR InterPro; IPR002817; ThiC/BzaA/B.
DR PANTHER; PTHR30557; PTHR30557; 1.
DR Pfam; PF01964; ThiC_Rad_SAM; 1.
DR SFLD; SFLDF00407; phosphomethylpyrimidine_syntha; 1.
DR TIGRFAMs; TIGR00190; thiC; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Cobalamin biosynthesis; Iron; Iron-sulfur; Lyase; Metal-binding;
KW Reference proteome; S-adenosyl-L-methionine; Zinc.
FT CHAIN 1..435
FT /note="5-hydroxybenzimidazole synthase"
FT /id="PRO_0000242265"
FT BINDING 95
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9A6Q5"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9A6Q5"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9A6Q5"
FT BINDING 186..188
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9A6Q5"
FT BINDING 227..230
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9A6Q5"
FT BINDING 266
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9A6Q5"
FT BINDING 270
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9A6Q5"
FT BINDING 293
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9A6Q5"
FT BINDING 334
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9A6Q5"
FT BINDING 410
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:Q9A6Q5"
FT BINDING 413
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:Q9A6Q5"
FT BINDING 417
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:Q9A6Q5"
SQ SEQUENCE 435 AA; 47670 MW; 447CF9C2A79BDCB5 CRC64;
MKTQIEIARE GTISSQMMAV AAEEHVSPDY VRQMVAEGKI VIPGNHSRKP RAVGIGKGLR
TKVNASIGTS SDIIDYGAEV RKALAAQEAG ADTLMELSVG GDLDRVRREV IAAVDLPVGN
VPLYQAFCEA ARKYGDPNKL DPEMLFDLIE KQCEDGMAFM AVHCGINLYT IERLKRQGYR
YGGLVSKGGV SMVAWMMANR RENPLYEQFD RVTSILRKYD TVLSLGNGLR AGAIHDSSDR
AQIQELLINC ELAELGREMG CQMLVEGPGH VPLDEVEGNI QLQKRMSGGA PYYMLGPIST
DVAPGFDHIT AAIGAAQSSR YGADLICYIT PAEHLALPNE EDVRQGVKAA KIAAYIGDMN
KYPERGRERD KEMSKARRDL DWKKQFELAL FPEDAKAIRA SRTPEDEATC TMCGDFCASR
GAGKLFAADL RGDKI
