BZAB_MOOTA
ID BZAB_MOOTA Reviewed; 426 AA.
AC Q2RHR5;
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 BzaB {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:A0A0K1TQ05};
GN Name=bzaB {ECO:0000303|PubMed:26246619}; OrderedLocusNames=Moth_1722;
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 BzaA, 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 BzaA for catalytic activity, as BzaB alone displays no
CC activity (By similarity). {ECO:0000250|UniProtKB:A0A0K1TQ05,
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:A0A0K1TQ05};
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}.
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DR EMBL; KT347436; AKV89417.1; -; Genomic_DNA.
DR EMBL; CP000232; ABC20024.1; -; Genomic_DNA.
DR RefSeq; WP_011393224.1; NC_007644.1.
DR RefSeq; YP_430567.1; NC_007644.1.
DR AlphaFoldDB; Q2RHR5; -.
DR SMR; Q2RHR5; -.
DR STRING; 264732.Moth_1722; -.
DR EnsemblBacteria; ABC20024; ABC20024; Moth_1722.
DR KEGG; mta:Moth_1722; -.
DR PATRIC; fig|264732.11.peg.1865; -.
DR eggNOG; COG0422; Bacteria.
DR HOGENOM; CLU_013181_2_2_9; -.
DR OMA; FMAIHTG; -.
DR BioCyc; MetaCyc:MON-20983; -.
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..426
FT /note="5-hydroxybenzimidazole synthase BzaB"
FT /id="PRO_0000242273"
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 265
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 407
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 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 414
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 426 AA; 45580 MW; 2BA3A21E20F5AFE2 CRC64;
MSQVLDARAG KITPEMEKVA ADEKVDVEFV RAGVAEGTIV IPRNTNRKVL KPCGIGRGLR
IKVNALIGTS SDRDDRQMEM RKIAAAEAAG CDSFMDLSTG GDIDEMRRLT LAHARVPVGS
VPIYQAAIEA IEKRGSIVAM TPDDMFAAVE KQARDGIDFM AIHSALNFEI LERLQASGRV
TDIVSRGGAF LTGWMLHNQK ENPLYEQFDR LLEILLKYDV TLSLGDAIRP GSTADSLDGA
QLQGMIVAGE LVRRAREAGV QVMVEGPGHV PLNHVETTMK LQKSLCGGAP YFILGTLATD
VAPGYDHITA AIGGALAGTV GADFICYVTP AEHLGLPTEQ DVKEGVIAAR IAAHAADLAR
GNRQAWERDL QMARARVALD VEKQISLAID QEKARSLLDG TGEDGVCAAC GTNCAALVAA
RYFGMN
