COBT_YERE8
ID COBT_YERE8 Reviewed; 352 AA.
AC A1JTP8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Nicotinate-nucleotide--dimethylbenzimidazole phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00230};
DE Short=NN:DBI PRT {ECO:0000255|HAMAP-Rule:MF_00230};
DE EC=2.4.2.21 {ECO:0000255|HAMAP-Rule:MF_00230};
DE AltName: Full=N(1)-alpha-phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00230};
GN Name=cobT {ECO:0000255|HAMAP-Rule:MF_00230}; OrderedLocusNames=YE2707;
OS Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS 8081).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=393305;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 13174 / 8081;
RX PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA Prentice M.B.;
RT "The complete genome sequence and comparative genome analysis of the high
RT pathogenicity Yersinia enterocolitica strain 8081.";
RL PLoS Genet. 2:2039-2051(2006).
CC -!- FUNCTION: Catalyzes the synthesis of alpha-ribazole-5'-phosphate from
CC nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB).
CC {ECO:0000255|HAMAP-Rule:MF_00230}.
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:0000255|HAMAP-Rule:MF_00230};
CC -!- PATHWAY: Nucleoside biosynthesis; alpha-ribazole biosynthesis; alpha-
CC ribazole from 5,6-dimethylbenzimidazole: step 1/2. {ECO:0000255|HAMAP-
CC Rule:MF_00230}.
CC -!- SIMILARITY: Belongs to the CobT family. {ECO:0000255|HAMAP-
CC Rule:MF_00230}.
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DR EMBL; AM286415; CAL12740.1; -; Genomic_DNA.
DR RefSeq; WP_005168498.1; NC_008800.1.
DR RefSeq; YP_001006897.1; NC_008800.1.
DR PDB; 6B5F; X-ray; 1.95 A; A/B=1-352.
DR PDBsum; 6B5F; -.
DR AlphaFoldDB; A1JTP8; -.
DR SMR; A1JTP8; -.
DR STRING; 393305.YE2707; -.
DR EnsemblBacteria; CAL12740; CAL12740; YE2707.
DR KEGG; yen:YE2707; -.
DR PATRIC; fig|393305.7.peg.2876; -.
DR eggNOG; COG2038; Bacteria.
DR HOGENOM; CLU_002982_0_0_6; -.
DR OMA; AIWYAGW; -.
DR UniPathway; UPA00061; UER00516.
DR Proteomes; UP000000642; Chromosome.
DR GO; GO:0008939; F:nicotinate-nucleotide-dimethylbenzimidazole phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
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 HAMAP; MF_00230; CobT; 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 Pfam; PF02277; DBI_PRT; 1.
DR SUPFAM; SSF52733; SSF52733; 1.
DR TIGRFAMs; TIGR03160; cobT_DBIPRT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cobalamin biosynthesis; Glycosyltransferase; Transferase.
FT CHAIN 1..352
FT /note="Nicotinate-nucleotide--dimethylbenzimidazole
FT phosphoribosyltransferase"
FT /id="PRO_1000021643"
FT ACT_SITE 316
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00230"
FT HELIX 4..9
FT /evidence="ECO:0007829|PDB:6B5F"
FT HELIX 16..27
FT /evidence="ECO:0007829|PDB:6B5F"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:6B5F"
FT TURN 33..36
FT /evidence="ECO:0007829|PDB:6B5F"
FT HELIX 37..47
FT /evidence="ECO:0007829|PDB:6B5F"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:6B5F"
FT HELIX 70..74
FT /evidence="ECO:0007829|PDB:6B5F"
FT HELIX 83..93
FT /evidence="ECO:0007829|PDB:6B5F"
FT HELIX 97..104
FT /evidence="ECO:0007829|PDB:6B5F"
FT STRAND 107..115
FT /evidence="ECO:0007829|PDB:6B5F"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:6B5F"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:6B5F"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:6B5F"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:6B5F"
FT HELIX 144..163
FT /evidence="ECO:0007829|PDB:6B5F"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:6B5F"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:6B5F"
FT HELIX 179..190
FT /evidence="ECO:0007829|PDB:6B5F"
FT HELIX 194..197
FT /evidence="ECO:0007829|PDB:6B5F"
FT TURN 201..203
FT /evidence="ECO:0007829|PDB:6B5F"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:6B5F"
FT HELIX 209..223
FT /evidence="ECO:0007829|PDB:6B5F"
FT HELIX 230..237
FT /evidence="ECO:0007829|PDB:6B5F"
FT HELIX 240..255
FT /evidence="ECO:0007829|PDB:6B5F"
FT HELIX 264..276
FT /evidence="ECO:0007829|PDB:6B5F"
FT HELIX 278..283
FT /evidence="ECO:0007829|PDB:6B5F"
FT HELIX 295..302
FT /evidence="ECO:0007829|PDB:6B5F"
FT HELIX 318..336
FT /evidence="ECO:0007829|PDB:6B5F"
SQ SEQUENCE 352 AA; 36408 MW; F5F4F8ABDBD88A96 CRC64;
MQTLSSILRT IAPLDSKAMA RATTRLDGLL KPQGSLGRLE QLAIQLAGMR GLYGHQVDRK
QIIVMAADHG VYDEGVAISP RVVTMVQALN MVRGVTGVCV LAANAGAEVK IVDVGIDSDT
LPGVIDMKVA RGSGNIARGA AMTRQQAEDL LIASATLTLQ QAAGGVKVFG VGELGMANTT
PAAAMVSVFT DSDPELAVGI GANFPSEQLH HKVAVVRRAI ETNQPDASDG IDVLAKVGGF
DLVGMTGVML GAAAAGLPVV LDGFLSYASA LAACRIEAKV RDYLIPSHLS AEKGAVIALN
HLQLEPYLQM GMRLGEGSGA ALAMHLVDAA CAMYNNMGSL AESNIELPGC VN
