BZAA_MOOTA
ID BZAA_MOOTA Reviewed; 432 AA.
AC Q2RHR4;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=5-hydroxybenzimidazole synthase BzaA {ECO:0000305|PubMed:26246619};
DE Short=5-OHBza synthase {ECO:0000305|PubMed:26246619};
DE Short=HBI synthase;
DE EC=4.1.99.23 {ECO:0000250|UniProtKB:A0A0K1TPY7};
GN Name=bzaA {ECO:0000303|PubMed:26246619}; OrderedLocusNames=Moth_1723;
OS Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Moorella group; Moorella.
OX NCBI_TaxID=264732;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 39073 / JCM 9320;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39073 / JCM 9320;
RX PubMed=18631365; DOI=10.1111/j.1462-2920.2008.01679.x;
RA Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C.,
RA Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.;
RT "The complete genome sequence of Moorella thermoacetica (f. Clostridium
RT thermoaceticum).";
RL Environ. Microbiol. 10:2550-2573(2008).
CC -!- FUNCTION: Together with BzaB, probably catalyzes the conversion of
CC aminoimidazole ribotide (AIR) to 5-hydroxybenzimidazole (5-HBI) in a
CC radical S-adenosyl-L-methionine (SAM)-dependent reaction. Is thus
CC involved in the anaerobic biosynthesis of the benzimidazole lower axial
CC ligand of the cobamide produced by M.thermoacetica (PubMed:26246619).
CC Requires BzaB for catalytic activity, as BzaA alone displays no
CC activity (By similarity). {ECO:0000250|UniProtKB:A0A0K1TPY7,
CC 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:0000250|UniProtKB:A0A0K1TPY7};
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 -!- SIMILARITY: Belongs to the ThiC family. 5-hydroxybenzimidazole synthase
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KT347436; AKV89416.1; -; Genomic_DNA.
DR EMBL; CP000232; ABC20025.1; -; Genomic_DNA.
DR RefSeq; WP_011393225.1; NC_007644.1.
DR RefSeq; YP_430568.1; NC_007644.1.
DR AlphaFoldDB; Q2RHR4; -.
DR SMR; Q2RHR4; -.
DR STRING; 264732.Moth_1723; -.
DR EnsemblBacteria; ABC20025; ABC20025; Moth_1723.
DR KEGG; mta:Moth_1723; -.
DR PATRIC; fig|264732.11.peg.1866; -.
DR eggNOG; COG0422; Bacteria.
DR HOGENOM; CLU_013181_2_2_9; -.
DR OMA; PYFVFGP; -.
DR BioCyc; MetaCyc:MON-20982; -.
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 S-adenosyl-L-methionine; Zinc.
FT CHAIN 1..432
FT /note="5-hydroxybenzimidazole synthase BzaA"
FT /id="PRO_0000242274"
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 185..187
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9A6Q5"
FT BINDING 226..229
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9A6Q5"
FT BINDING 269
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9A6Q5"
FT BINDING 292
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9A6Q5"
FT BINDING 333
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9A6Q5"
FT BINDING 409
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 412
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 416
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 432 AA; 46398 MW; 63699728AAB40360 CRC64;
MNLIESARAG LITPEMEQVA VQEGVTPEFV RQGVADGTIV ILRNARRQNV TPVGVGKGLR
TKVSASVGLY GETGGIDVEV AKIKAAVEAG TDAIMDLSVS GDIEAMLAET LAVSPKPVGT
LPLYQAMAEA GRKYGSSVNM RDEDLFDVIE RHAAAGVDFL ALHCGTTMNI VERARNEGRI
DPLVSYGGSH LIGWMLANRR ENPLYEHFDR VLAIARKYDV TISFADGMRP GCLADSLDGP
QVEELVVLGE LVRRAREAGV QVMVKGPGHV PLQQLKATVV LEKSLCHGAP YFVFGPLVTD
IAIGYDHINA AIGGALSAWA GAEFLCYVTA AEHVGIPDID QVREGVIAAR IAAHAADLAN
GLTCAREWDR ELSRARKELD WKRQIALAID PERAGRLREE RSDAAAAGCA MCGKYCAMEI
VSRYLGTARH TC
