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Database: UniProt
Entry: A0A074M711_9BACL
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ID   A0A074M711_9BACL        Unreviewed;       248 AA.
AC   A0A074M711;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Adenosylcobinamide kinase {ECO:0000256|ARBA:ARBA00029570};
DE            EC=2.7.1.156 {ECO:0000256|ARBA:ARBA00012016};
DE            EC=2.7.7.62 {ECO:0000256|ARBA:ARBA00012523};
DE   AltName: Full=Adenosylcobinamide-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00030571};
GN   ORFNames=EL26_18315 {ECO:0000313|EMBL:KEO81797.1};
OS   Tumebacillus flagellatus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC   Tumebacillus.
OX   NCBI_TaxID=1157490 {ECO:0000313|EMBL:KEO81797.1, ECO:0000313|Proteomes:UP000027931};
RN   [1] {ECO:0000313|EMBL:KEO81797.1, ECO:0000313|Proteomes:UP000027931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GST4 {ECO:0000313|EMBL:KEO81797.1,
RC   ECO:0000313|Proteomes:UP000027931};
RX   PubMed=23435245; DOI=10.1099/ijs.0.045351-0;
RA   Wang Q., Xie N., Qin Y., Shen N., Zhu J., Mi H., Huang R.;
RT   "Tumebacillus flagellatus sp. nov., an alpha-amylase/pullulanase-producing
RT   bacterium isolated from cassava wastewater.";
RL   Int. J. Syst. Evol. Microbiol. 63:3138-3142(2013).
CC   -!- FUNCTION: Catalyzes ATP-dependent phosphorylation of adenosylcobinamide
CC       and addition of GMP to adenosylcobinamide phosphate.
CC       {ECO:0000256|ARBA:ARBA00003889}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosylcob(III)inamide + ATP = adenosylcob(III)inamide
CC         phosphate + ADP + H(+); Xref=Rhea:RHEA:15769, ChEBI:CHEBI:2480,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58502,
CC         ChEBI:CHEBI:456216; EC=2.7.1.156;
CC         Evidence={ECO:0000256|ARBA:ARBA00000312};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosylcob(III)inamide + GTP = adenosylcob(III)inamide
CC         phosphate + GDP + H(+); Xref=Rhea:RHEA:15765, ChEBI:CHEBI:2480,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:58189,
CC         ChEBI:CHEBI:58502; EC=2.7.1.156;
CC         Evidence={ECO:0000256|ARBA:ARBA00001522};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosylcob(III)inamide phosphate + GTP + H(+) =
CC         adenosylcob(III)inamide-GDP + diphosphate; Xref=Rhea:RHEA:22712,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:58502, ChEBI:CHEBI:60487; EC=2.7.7.62;
CC         Evidence={ECO:0000256|ARBA:ARBA00000711};
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       adenosylcobalamin from cob(II)yrinate a,c-diamide: step 5/7.
CC       {ECO:0000256|ARBA:ARBA00005159}.
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       adenosylcobalamin from cob(II)yrinate a,c-diamide: step 6/7.
CC       {ECO:0000256|ARBA:ARBA00004692}.
CC   -!- SIMILARITY: Belongs to the CobU/CobP family.
CC       {ECO:0000256|ARBA:ARBA00007490}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KEO81797.1}.
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DR   EMBL; JMIR01000031; KEO81797.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A074M711; -.
DR   STRING; 1157490.EL26_18315; -.
DR   eggNOG; COG2087; Bacteria.
DR   OrthoDB; 9799422at2; -.
DR   UniPathway; UPA00148; UER00236.
DR   Proteomes; UP000027931; Unassembled WGS sequence.
DR   GO; GO:0043752; F:adenosylcobinamide kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008820; F:cobinamide phosphate guanylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00544; CobU; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003203; CobU/CobP.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR34848; -; 1.
DR   PANTHER; PTHR34848:SF1; BIFUNCTIONAL ADENOSYLCOBALAMIN BIOSYNTHESIS PROTEIN COBU; 1.
DR   Pfam; PF02283; CobU; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027931};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ   SEQUENCE   248 AA;  27668 MW;  3EEFF1E974E2501F CRC64;
     MPYTLITGGV RSGKSAWAER VAGLSRRVLY VATGQVWDEE MERRIDVHRD RRPAQWGLLE
     VQAELAEPLM EAMQDAGQPW EGVLIDDLST WVSTVLLQLP EEEWRSEGTR NRLFNEATQL
     AARLRQSSVP ATVVTNETGL GGVALTPLGR AFQDLLGVVN QIFAAQAEDV YLVVSGRPLK
     LPNVEETFLE EKRNEHHPEN ASLIEEQSNE WFSGSAERMS QGTPNTKVFS FEESFSQIDL
     ASRGGTDL
//
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