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Database: UniProt
Entry: A0A1A9F4J8_9GAMM
LinkDB: A0A1A9F4J8_9GAMM
Original site: A0A1A9F4J8_9GAMM 
ID   A0A1A9F4J8_9GAMM        Unreviewed;       351 AA.
AC   A0A1A9F4J8;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Nicotinate-nucleotide--dimethylbenzimidazole phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00015486, ECO:0000256|HAMAP-Rule:MF_00230};
DE            Short=NN:DBI PRT {ECO:0000256|HAMAP-Rule:MF_00230};
DE            EC=2.4.2.21 {ECO:0000256|ARBA:ARBA00011991, ECO:0000256|HAMAP-Rule:MF_00230};
DE   AltName: Full=N(1)-alpha-phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00030686, ECO:0000256|HAMAP-Rule:MF_00230};
GN   Name=cobT {ECO:0000256|HAMAP-Rule:MF_00230};
GN   ORFNames=A8C75_05895 {ECO:0000313|EMBL:ANG65115.1};
OS   Marinobacterium aestuarii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinobacterium.
OX   NCBI_TaxID=1821621 {ECO:0000313|EMBL:ANG65115.1, ECO:0000313|Proteomes:UP000078070};
RN   [1] {ECO:0000313|Proteomes:UP000078070}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ST58-10 {ECO:0000313|Proteomes:UP000078070};
RA   Baek K., Yang S.-J.;
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ANG65115.1, ECO:0000313|Proteomes:UP000078070}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ST58-10 {ECO:0000313|EMBL:ANG65115.1,
RC   ECO:0000313|Proteomes:UP000078070};
RX   PubMed=29303694; DOI=10.1099/ijsem.0.002561;
RA   Bae S.S., Jung J., Chung D., Baek K.;
RT   "Marinobacterium aestuarii sp. nov., a benzene-degrading marine bacterium
RT   isolated from estuary sediment.";
RL   Int. J. Syst. Evol. Microbiol. 68:651-656(2018).
CC   -!- FUNCTION: Catalyzes the synthesis of alpha-ribazole-5'-phosphate from
CC       nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB).
CC       {ECO:0000256|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:0000256|ARBA:ARBA00001058, ECO:0000256|HAMAP-
CC         Rule:MF_00230};
CC   -!- PATHWAY: Nucleoside biosynthesis; alpha-ribazole biosynthesis; alpha-
CC       ribazole from 5,6-dimethylbenzimidazole: step 1/2.
CC       {ECO:0000256|ARBA:ARBA00005049, ECO:0000256|HAMAP-Rule:MF_00230}.
CC   -!- SIMILARITY: Belongs to the CobT family. {ECO:0000256|ARBA:ARBA00007110,
CC       ECO:0000256|HAMAP-Rule:MF_00230}.
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DR   EMBL; CP015839; ANG65115.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1A9F4J8; -.
DR   STRING; 1821621.A8C75_05895; -.
DR   KEGG; mars:A8C75_05895; -.
DR   UniPathway; UPA00061; UER00516.
DR   Proteomes; UP000078070; 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   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.
PE   3: Inferred from homology;
KW   Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573, ECO:0000256|HAMAP-
KW   Rule:MF_00230};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW   Rule:MF_00230}; Reference proteome {ECO:0000313|Proteomes:UP000078070};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00230}.
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        317
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00230"
SQ   SEQUENCE   351 AA;  36188 MW;  A063B4B9E5C52E3F CRC64;
     MAANWLEQPM QQPNAEAEDQ ARAHQLQLTK PAGALGELEQ LAIRLAGLQG RVYPRVDSCH
     ISLFAADHGI AAAGVSAYPQ AVTAQMLANF VSGGAAVAVL AKLAGARFDV VNLGTLQRPE
     PDPRVVDRWL GPGTADFTQQ AAMTVAQRDA ALLAGAERLA EAQKAGCELF VAGEMGIGNT
     SAATALGAVL LELDPAQLAG PGTGVNATVL AHKVALLRQG LSLHTGDNPR VLELLRRLGG
     FEIVAMVGAY LHAGQCGVPV LVDGFISTLA ALVAVRLNPA LAPWLLYGHR SAEPGHGLML
     EALQARPLLM LDMRLGEGSG AALALQIVRS ACELHSGMAT FAQAGVAGPG G
//
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