BZAF_DESAH
ID BZAF_DESAH Reviewed; 439 AA.
AC C0QJ00;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
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:0000250|UniProtKB:P61425};
GN Synonyms=thiC {ECO:0000312|EMBL:ACN13790.1}; OrderedLocusNames=HRM2_06760;
OS Desulforapulum autotrophicum (strain ATCC 43914 / DSM 3382 / VKM B-1955 /
OS HRM2) (Desulfobacterium autotrophicum).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC Desulfobacteraceae; Desulforapulum.
OX NCBI_TaxID=177437;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43914 / DSM 3382 / VKM B-1955 / HRM2;
RX PubMed=19187283; DOI=10.1111/j.1462-2920.2008.01825.x;
RA Strittmatter A.W., Liesegang H., Rabus R., Decker I., Amann J., Andres S.,
RA Henne A., Fricke W.F., Martinez-Arias R., Bartels D., Goesmann A.,
RA Krause L., Puehler A., Klenk H.P., Richter M., Schuler M., Gloeckner F.O.,
RA Meyerdierks A., Gottschalk G., Amann R.;
RT "Genome sequence of Desulfobacterium autotrophicum HRM2, a marine sulfate
RT reducer oxidizing organic carbon completely to carbon dioxide.";
RL Environ. Microbiol. 11:1038-1055(2009).
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 D.autotrophicum. {ECO:0000250|UniProtKB:P61425}.
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; CP001087; ACN13790.1; -; Genomic_DNA.
DR RefSeq; WP_012663038.1; NC_012108.1.
DR AlphaFoldDB; C0QJ00; -.
DR SMR; C0QJ00; -.
DR STRING; 177437.HRM2_06760; -.
DR PRIDE; C0QJ00; -.
DR EnsemblBacteria; ACN13790; ACN13790; HRM2_06760.
DR KEGG; dat:HRM2_06760; -.
DR eggNOG; COG0422; Bacteria.
DR HOGENOM; CLU_013181_2_2_7; -.
DR OMA; PYFVFGP; -.
DR OrthoDB; 505395at2; -.
DR Proteomes; UP000000442; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro.
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; IPR016176; Cbl-dep_enz_cat.
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 SUPFAM; SSF51703; SSF51703; 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..439
FT /note="5-hydroxybenzimidazole synthase"
FT /id="PRO_1000202650"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9A6Q5"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9A6Q5"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9A6Q5"
FT BINDING 187..189
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9A6Q5"
FT BINDING 228..231
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9A6Q5"
FT BINDING 267
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9A6Q5"
FT BINDING 271
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9A6Q5"
FT BINDING 294
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9A6Q5"
FT BINDING 335
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 439 AA; 48307 MW; EB179E74598CCAEB CRC64;
MKTQIELARD GIISRQMEQV AADENFNPEI IRTRVAAGEI VIPCNPNRTN QKVVGIGTGL
RTKINASIGT SSDICSIENE VQKAIAIEEE GADTLMELSA GGNLDKVRQE VLKAVNLPVG
NVPLYQAFKE TGRKYNDPSK LDPEFLFDLI ERQLSDGLSF MAIHCGINQY TIERLRKQGF
RYGGLASKGG TFMVAWMDAT GKENPLYEQF DRVCTLMKKY DAVLSLGNGI RAGAIHDSHD
RAQMAEMIIN CELAELGREQ GCQMMVEGPG HVPLDEIQAN IILEKRMSGN APYYVLGPIP
ADTGAGYDHI TSAIGAASST WHGADLICYI TPAEHLALPT EADVREGVRA TKLAVRIGDI
AKYPDRRENE RLASMARRDM RWDDLEQHLL FPDIARKTRA SRAPEDGGTC TMCGDFCAMK
KGNEIFKDDI KNDKIAPGA
