BZAF_GEOSL
ID BZAF_GEOSL Reviewed; 435 AA.
AC P61425;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=5-hydroxybenzimidazole synthase {ECO:0000303|PubMed:26246619};
DE Short=5-OHBza synthase {ECO:0000303|PubMed:26246619};
DE Short=HBI synthase;
DE EC=4.1.99.23 {ECO:0000269|PubMed:26246619};
GN Name=bzaF {ECO:0000303|PubMed:26246619};
GN Synonyms=thiC-2 {ECO:0000312|EMBL:AAR36397.1}; OrderedLocusNames=GSU3005;
OS Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=243231;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51573 / DSM 12127 / PCA;
RX PubMed=14671304; DOI=10.1126/science.1088727;
RA Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C.,
RA Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J.,
RA Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA Gwinn M.L., Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J.,
RA Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A.,
RA Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R., Van Aken S.E.,
RA Lovley D.R., Fraser C.M.;
RT "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT environments.";
RL Science 302:1967-1969(2003).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND PATHWAY.
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.sulfurreducens. {ECO:0000269|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:0000269|PubMed:26246619};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:26246619};
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:Q9A6Q5}.
CC -!- SIMILARITY: Belongs to the ThiC family. 5-hydroxybenzimidazole synthase
CC subfamily. {ECO:0000305}.
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DR EMBL; AE017180; AAR36397.1; -; Genomic_DNA.
DR RefSeq; NP_954047.1; NC_002939.5.
DR RefSeq; WP_010943635.1; NC_002939.5.
DR AlphaFoldDB; P61425; -.
DR SMR; P61425; -.
DR STRING; 243231.GSU3005; -.
DR PRIDE; P61425; -.
DR EnsemblBacteria; AAR36397; AAR36397; GSU3005.
DR KEGG; gsu:GSU3005; -.
DR PATRIC; fig|243231.5.peg.3032; -.
DR eggNOG; COG0422; Bacteria.
DR HOGENOM; CLU_013181_2_2_7; -.
DR InParanoid; P61425; -.
DR OMA; PYFVFGP; -.
DR BioCyc; MetaCyc:MON-20980; -.
DR Proteomes; UP000000577; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
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 1: Evidence at protein level;
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_0000152808"
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; 47750 MW; E6F4F2FC1C9882A0 CRC64;
MKTQIEQARE GIITPQMAAV AAEEHVSPEY VCRMVAEGKV VIPWNHVRAP KAVGIGKGLR
TKVNASIGTS SDIVDYEAEV RKARAAQESG ADTLMELSVG GDLDRVRREV IAAVDLPVGN
VPLYQAFCEA ARKYGDPNRL DPEMLFDLIE RQCADGMAFM AVHCGINLYT IERLRRQGYR
YGGLVSKGGV SMVGWMMANG RENPLYEQFD RVVGILKKYD TVLSLGNGLR AGAIHDSSDR
AQIQELLINC ELAEMGREMG CQMLVEGPGH VPLDEVEGNI QLQKRMSGGA PYYMLGPIST
DVAPGFDHIT AAIGAAQSSR FGADLICYIT PAEHLALPNE EDVRQGVKAA RVAAYIGDMN
KYPEKGRERD REMSKARRDL DWQRQFELAL YPEDARAIRA SRTPEDEATC TMCGDFCASR
GAGRLFAGDL RGDKV
