ID   A0A3D2XQM5_9FIRM        Unreviewed;       126 AA.
AC   A0A3D2XQM5;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   10-FEB-2021, entry version 10.
DE   RecName: Full=Adenosylcobinamide kinase {ECO:0000256|ARBA:ARBA00014853};
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:ARBA00020787};
GN   ORFNames=DHW25_04670 {ECO:0000313|EMBL:HCL09177.1};
OS   Blautia sp.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; Blautia;
OC   unclassified Blautia.
OX   NCBI_TaxID=1955243 {ECO:0000313|EMBL:HCL09177.1, ECO:0000313|Proteomes:UP000262112};
RN   [1] {ECO:0000313|EMBL:HCL09177.1, ECO:0000313|Proteomes:UP000262112}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UBA9114 {ECO:0000313|EMBL:HCL09177.1};
RX   PubMed=30148503; DOI=.1038/nbt.4229;
RA   Parks D.H., Chuvochina M., Waite D.W., Rinke C., Skarshewski A.,
RA   Chaumeil P.A., Hugenholtz P.;
RT   "A standardized bacterial taxonomy based on genome phylogeny substantially
RT   revises the tree of life.";
RL   Nat. Biotechnol. 36:996-1004(2018).
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 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:HCL09177.1}.
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DR   EMBL; DPVL01000023; HCL09177.1; -; Genomic_DNA.
DR   UniPathway; UPA00148; UER00237.
DR   Proteomes; UP000262112; 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   InterPro; IPR003203; Cobinamide_kinase/P_G-Trfase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF02283; CobU; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:HCL09177.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ   SEQUENCE   126 AA;  13778 MW;  EA740FE24AD54C8D CRC64;
     MEMIIGGAFQ GKSDYAKEKH PEICWKNGGK LEEYQLMKAE GVLDFQEFIR KELKAGHDVA
     GLAEKLAEGN PDIVVVSQEV GYGVVPMDAF DRKYREAVGR VCTGLASKSK KVTRVVCGIG
     TVIKDA
//