ID A0A1I3ZHE4_9FIRM Unreviewed; 345 AA.
AC A0A1I3ZHE4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Pyroglutamyl-peptidase I {ECO:0000256|PROSITE-ProRule:PRU10076};
DE EC=3.4.19.3 {ECO:0000256|PROSITE-ProRule:PRU10076};
GN ORFNames=SAMN05216390_10175 {ECO:0000313|EMBL:SFK43091.1};
OS Lachnospiraceae bacterium KH1T2.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1855374 {ECO:0000313|EMBL:SFK43091.1, ECO:0000313|Proteomes:UP000198626};
RN [1] {ECO:0000313|EMBL:SFK43091.1, ECO:0000313|Proteomes:UP000198626}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KH1T2 {ECO:0000313|EMBL:SFK43091.1,
RC ECO:0000313|Proteomes:UP000198626};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dimethylbenzimidazole + nicotinate beta-D-ribonucleotide =
CC alpha-ribazole 5'-phosphate + H(+) + nicotinate;
CC Xref=Rhea:RHEA:11196, ChEBI:CHEBI:15378, ChEBI:CHEBI:15890,
CC ChEBI:CHEBI:32544, ChEBI:CHEBI:57502, ChEBI:CHEBI:57918; EC=2.4.2.21;
CC Evidence={ECO:0000256|ARBA:ARBA00001058};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal pyroglutamyl group from a
CC polypeptide, the second amino acid generally not being Pro.;
CC EC=3.4.19.3; Evidence={ECO:0000256|PROSITE-ProRule:PRU10076};
CC -!- PATHWAY: Nucleoside biosynthesis; alpha-ribazole biosynthesis; alpha-
CC ribazole from 5,6-dimethylbenzimidazole: step 1/2.
CC {ECO:0000256|ARBA:ARBA00005049}.
CC -!- SIMILARITY: Belongs to the CobT family.
CC {ECO:0000256|ARBA:ARBA00007110}.
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DR EMBL; FOSY01000001; SFK43091.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3ZHE4; -.
DR STRING; 1855374.SAMN05216390_10175; -.
DR UniPathway; UPA00061; UER00516.
DR Proteomes; UP000198626; Unassembled WGS sequence.
DR GO; GO:0008939; F:nicotinate-nucleotide-dimethylbenzimidazole phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016920; F:pyroglutamyl-peptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd02439; DMB-PRT_CobT; 1.
DR Gene3D; 1.10.1610.10; -; 1.
DR Gene3D; 3.40.50.10210; -; 1.
DR InterPro; IPR003200; Nict_dMeBzImd_PRibTrfase.
DR InterPro; IPR017846; Nict_dMeBzImd_PRibTrfase_bact.
DR InterPro; IPR023195; Nict_dMeBzImd_PRibTrfase_N.
DR InterPro; IPR036087; Nict_dMeBzImd_PRibTrfase_sf.
DR InterPro; IPR033693; PGPEP1_Glu_AS.
DR NCBIfam; TIGR03160; cobT_DBIPRT; 1.
DR PANTHER; PTHR43463; NICOTINATE-NUCLEOTIDE--DIMETHYLBENZIMIDAZOLE PHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR43463:SF1; NICOTINATE-NUCLEOTIDE--DIMETHYLBENZIMIDAZOLE PHOSPHORIBOSYLTRANSFERASE; 1.
DR Pfam; PF02277; DBI_PRT; 1.
DR SUPFAM; SSF52733; Nicotinate mononucleotide:5,6-dimethylbenzimidazole phosphoribosyltransferase (CobT); 1.
DR PROSITE; PS01333; PYRASE_GLU; 1.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000313|EMBL:SFK43091.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198626};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SFK43091.1}.
FT ACT_SITE 268
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10076"
SQ SEQUENCE 345 AA; 36600 MW; 6E5CF9357FC276AB CRC64;
MIKINNPSKE VYEKAKKRWD SIAKPLDGMG RFEEIISGIA AIQNTTDVSI DKKCVLVMCA
DNGIVAENIS QSGQEVTAVC AKKMAEGTTS VCRMAQKIGA DIIPVDIGIV SEVNQKGVLQ
KNVRRGTRNF ALEPAMTAEE CRKAIDIGIA LVKEYAQKGY NMIATGEMGI GNTTTSSAVA
AALTGLEVRT VTGRGAGLDD DRLKNKIAVI EKAIDKYSLR NADAMKILQC VGGLDIAGLV
GVCIGGAEAG VPIVLDGIIA DVAALTAERI APGVKDYLIP SHIGKEPAAI HLNRLLGFEP
VIHANMALGE GTGAVVMMGM LDIAMTVYDS CELFDDIAVD QYERF
//
