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Entry: A0A1M4X010_9BACT
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ID   A0A1M4X010_9BACT        Unreviewed;       170 AA.
AC   A0A1M4X010;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
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=SAMN05444362_102365 {ECO:0000313|EMBL:SHE86804.1};
OS   Dysgonomonas macrotermitis.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Dysgonomonadaceae;
OC   Dysgonomonas.
OX   NCBI_TaxID=1346286 {ECO:0000313|EMBL:SHE86804.1, ECO:0000313|Proteomes:UP000184480};
RN   [1] {ECO:0000313|Proteomes:UP000184480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27370 {ECO:0000313|Proteomes:UP000184480};
RA   Varghese N., Submissions S.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; FQUC01000002; SHE86804.1; -; Genomic_DNA.
DR   RefSeq; WP_062176043.1; NZ_FQUC01000002.1.
DR   AlphaFoldDB; A0A1M4X010; -.
DR   STRING; 1346286.SAMN05444362_102365; -.
DR   OrthoDB; 9799422at2; -.
DR   UniPathway; UPA00148; UER00236.
DR   Proteomes; UP000184480; 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:0005525; F:GTP binding; IEA:UniProtKB-KW.
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   PIRSF; PIRSF006135; 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   GTP-binding {ECO:0000256|PIRSR:PIRSR006135-2};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SHE86804.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRSR:PIRSR006135-2};
KW   Nucleotidyltransferase {ECO:0000313|EMBL:SHE86804.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184480};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SHE86804.1}.
FT   ACT_SITE        51
FT                   /note="GMP-histidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006135-1"
FT   BINDING         10..17
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006135-2"
FT   BINDING         35..37
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006135-2"
FT   BINDING         63
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006135-2"
FT   BINDING         81
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006135-2"
SQ   SEQUENCE   170 AA;  19527 MW;  9366F2A9D9C9CD7A CRC64;
     MNKKITLITG GQRSGKSSYA EKLALSLSPN PVYLATSRIW DEEHQKRIER HQADRGPEWT
     NIEEEKYLSN HNLNNRIVLI DCITLWATNF FFDNDSNVKK SLDELKSEFD KFTSQEAHFI
     FVTNEIGLGG TSENQIQRLF TDLQGWVNQY VASKADEVFL MVSGIPLKVK
//
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