BZAF_DESA6
ID BZAF_DESA6 Reviewed; 435 AA.
AC Q1JZW3;
DT 27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=5-hydroxybenzimidazole synthase {ECO:0000303|PubMed:26237670};
DE Short=HBI synthase {ECO:0000303|PubMed:26237670};
DE EC=4.1.99.23 {ECO:0000269|PubMed:26237670};
GN Name=bzaF {ECO:0000303|PubMed:26237670};
GN ORFNames=Dace_2479 {ECO:0000312|EMBL:EAT15779.1};
OS Desulfuromonas acetoxidans (strain DSM 684 / 11070).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Desulfuromonadaceae; Desulfuromonas.
OX NCBI_TaxID=281689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 684 / 11070;
RG US DOE Joint Genome Institute (JGI-ORNL);
RA Larimer F., Land M., Hauser L.;
RT "Annotation of the draft genome assembly of Desulfuromonas acetoxidans DSM
RT 684.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 684 / 11070;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Bruce D.,
RA Pitluck S., Richardson P.;
RT "Sequencing of the draft genome and assembly of Desulfuromonas acetoxidans
RT DSM 684.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, REACTION MECHANISM, AND
RP 3D-STRUCTURE MODELING.
RC STRAIN=DSM 684 / 11070;
RX PubMed=26237670; DOI=10.1021/jacs.5b03576;
RA Mehta A.P., Abdelwahed S.H., Fenwick M.K., Hazra A.B., Taga M.E., Zhang Y.,
RA Ealick S.E., Begley T.P.;
RT "Anaerobic 5-hydroxybenzimidazole formation from aminoimidazole ribotide:
RT an unanticipated intersection of thiamin and vitamin B12 biosynthesis.";
RL J. Am. Chem. Soc. 137:10444-10447(2015).
CC -!- FUNCTION: Catalyzes the complex conversion of aminoimidazole ribotide
CC (AIR) to 5-hydroxybenzimidazole (5-HBI) in a radical S-adenosyl-L-
CC methionine (SAM)-dependent reaction. Is thus involved in the anaerobic
CC biosynthesis of dimethylbenzimidazole (DMB), the lower axial ligand of
CC vitamin B12 (cobalamin). {ECO:0000269|PubMed:26237670}.
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:26237670};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:26237670};
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 -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC {ECO:0000305|PubMed:26237670}.
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; AAEW02000008; EAT15779.1; -; Genomic_DNA.
DR RefSeq; WP_006000218.1; NZ_AAEW02000008.1.
DR AlphaFoldDB; Q1JZW3; -.
DR SMR; Q1JZW3; -.
DR EnsemblBacteria; EAT15779; EAT15779; Dace_2479.
DR OrthoDB; 505395at2; -.
DR BioCyc; MetaCyc:MON-19551; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000005695; Unassembled WGS sequence.
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-UniPathway.
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 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_0000441709"
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; 48157 MW; 911278040763AF26 CRC64;
MKTQVEHAVD GIITEQMATV AHDEDLSPEY IRTMVAEGKI VIPNNSNSTP KPVGIGKGLR
TKVNASIGTS SDIVNYQAEV RKARIAEQAG ADTLMELSVG GNLDRVRREV LAAVNLPVGN
VPLYQAFCDA TRKYGSADKL DPEELFDLIE QQCEDGLAFM AIHCGINRYT IERLRKQHYR
YGGLVSKGGT SMVSWMEHNN RENPLYEQFD RVVAILKKYD VCLSLGNGLR AGAIHDSHDR
AQMQELIINC ELAQLGREMG CQMLVEGPGH MPLDEVEANI LIQKRMSNEA PYYMLGPIST
DVVPGFDHIS SAIGAAQSAR YGADLICYIT PAEHLALPNE DDVRSGVEAA RVATYIGDMN
KYPDKGRQRD KAMSKARRDL QWDKQFELAL MPEQARQVRD SRLPEEEHSC TMCGNFCAAN
GSKTLFDGDL QGDKC
