ID C6LEQ0_9FIRM Unreviewed; 183 AA.
AC C6LEQ0;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 47.
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 Name=cobU {ECO:0000313|EMBL:EET61033.1};
GN ORFNames=BRYFOR_07101 {ECO:0000313|EMBL:EET61033.1};
OS Marvinbryantia formatexigens DSM 14469.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Marvinbryantia.
OX NCBI_TaxID=478749 {ECO:0000313|EMBL:EET61033.1, ECO:0000313|Proteomes:UP000005561};
RN [1] {ECO:0000313|EMBL:EET61033.1, ECO:0000313|Proteomes:UP000005561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14469 {ECO:0000313|EMBL:EET61033.1,
RC ECO:0000313|Proteomes:UP000005561};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (JUL-2009) 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}.
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:EET61033.1}.
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DR EMBL; ACCL02000008; EET61033.1; -; Genomic_DNA.
DR AlphaFoldDB; C6LEQ0; -.
DR STRING; 168384.SAMN05660368_00292; -.
DR eggNOG; COG2087; Bacteria.
DR UniPathway; UPA00148; UER00236.
DR Proteomes; UP000005561; Unassembled WGS sequence.
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 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:0000313|EMBL:EET61033.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR006135-2};
KW Nucleotidyltransferase {ECO:0000313|EMBL:EET61033.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005561};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EET61033.1}.
FT ACT_SITE 54
FT /note="GMP-histidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006135-1"
FT BINDING 12..19
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR006135-2"
FT BINDING 55..58
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 86
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR006135-2"
SQ SEQUENCE 183 AA; 20356 MW; 145A4436DC85D47F CRC64;
MGDEKMFMVV TGGSGSGKSA WAEQQVLKLG EQKRYYIATM QCADEESRRR IERHRRMRAG
KHFQTLECPA DLERLFLEPG STALLECMSN LTANEFFDGK KHTPQETAAK IMTGVEKLKG
QCANLIVVTN EVFSDGAVFD EWTTQYLECL GSINCAMARM ADCVAEVVYG IPVILKQSGD
GEK
//
