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Database: UniProt
Entry: C8XJ17_NAKMY
LinkDB: C8XJ17_NAKMY
Original site: C8XJ17_NAKMY 
ID   C8XJ17_NAKMY            Unreviewed;       180 AA.
AC   C8XJ17;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 66.
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   OrderedLocusNames=Namu_0171 {ECO:0000313|EMBL:ACV76604.1};
OS   Nakamurella multipartita (strain ATCC 700099 / DSM 44233 / CIP 104796 / JCM
OS   9543 / NBRC 105858 / Y-104) (Microsphaera multipartita).
OC   Bacteria; Actinomycetota; Actinomycetes; Nakamurellales; Nakamurellaceae;
OC   Nakamurella.
OX   NCBI_TaxID=479431 {ECO:0000313|EMBL:ACV76604.1, ECO:0000313|Proteomes:UP000002218};
RN   [1] {ECO:0000313|Proteomes:UP000002218}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700099 / DSM 44233 / CIP 104796 / JCM 9543 / NBRC 105858 /
RC   Y-104 {ECO:0000313|Proteomes:UP000002218};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Ovchinnikova G., Sims D., Meincke L., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Nakamurella multipartita DSM 44233.";
RL   Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACV76604.1, ECO:0000313|Proteomes:UP000002218}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700099 / DSM 44233 / CIP 104796 / JCM 9543 / NBRC 105858 /
RC   Y-104 {ECO:0000313|Proteomes:UP000002218};
RX   PubMed=21304699;
RA   Tice H., Mayilraj S., Sims D., Lapidus A., Nolan M., Lucas S.,
RA   Glavina Del Rio T., Copeland A., Cheng J.F., Meincke L., Bruce D.,
RA   Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA   Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Detter J.C., Brettin T., Rohde M., Goker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Chen F.;
RT   "Complete genome sequence of Nakamurella multipartita type strain (Y-
RT   104).";
RL   Stand. Genomic Sci. 2:168-175(2010).
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; CP001737; ACV76604.1; -; Genomic_DNA.
DR   RefSeq; WP_012814079.1; NC_013235.1.
DR   AlphaFoldDB; C8XJ17; -.
DR   STRING; 479431.Namu_0171; -.
DR   KEGG; nml:Namu_0171; -.
DR   eggNOG; COG2087; Bacteria.
DR   HOGENOM; CLU_094161_0_1_11; -.
DR   InParanoid; C8XJ17; -.
DR   OrthoDB; 9788370at2; -.
DR   UniPathway; UPA00148; UER00236.
DR   Proteomes; UP000002218; Chromosome.
DR   GO; GO:0036429; F:adenosylcobinamide kinase (ATP-specific) activity; IEA:RHEA.
DR   GO; GO:0036428; F:adenosylcobinamide kinase (GTP-specific) activity; IEA:RHEA.
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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRSR:PIRSR006135-2};
KW   Nucleotidyltransferase {ECO:0000313|EMBL:ACV76604.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002218};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACV76604.1}.
FT   ACT_SITE        55
FT                   /note="GMP-histidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006135-1"
FT   BINDING         11..18
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         56..59
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006135-2"
FT   BINDING         67
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006135-2"
FT   BINDING         85
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006135-2"
SQ   SEQUENCE   180 AA;  20058 MW;  01238878C9526965 CRC64;
     MTSTRRTLVT GGVRSGKSRV AENLLADRPA VSYLAPGPVP DRSVDPEWAD RIDAHRAQRP
     SHWRTVETTD LARALGQERA AVLIDCLGTW VTAVVDQLGT WDRRLAEWQP DFDRQLDDLE
     RAWRSHPGPL VAVTNEVGWG VVPEHRSGRT FRDLLGRVNQ RIAAASDDVL LVVAGRTLRL
//
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