ID A0A367FDN1_9ACTN Unreviewed; 367 AA.
AC A0A367FDN1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=DQ384_24305 {ECO:0000313|EMBL:RCG28391.1};
OS Sphaerisporangium album.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Sphaerisporangium.
OX NCBI_TaxID=509200 {ECO:0000313|EMBL:RCG28391.1, ECO:0000313|Proteomes:UP000253094};
RN [1] {ECO:0000313|EMBL:RCG28391.1, ECO:0000313|Proteomes:UP000253094}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCTCC AA 208026 {ECO:0000313|EMBL:RCG28391.1,
RC ECO:0000313|Proteomes:UP000253094};
RA Li L.;
RT "Sphaerisporangium craniellae sp. nov., isolated from a marine sponge in
RT the South China Sea.";
RL Submitted (JUN-2018) 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:RCG28391.1}.
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DR EMBL; QOIL01000014; RCG28391.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367FDN1; -.
DR OrthoDB; 9788370at2; -.
DR UniPathway; UPA00148; UER00236.
DR Proteomes; UP000253094; 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 Kinase {ECO:0000313|EMBL:RCG28391.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000313|EMBL:RCG28391.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000253094};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RCG28391.1}.
SQ SEQUENCE 367 AA; 39241 MW; D0E0AF38AC61F926 CRC64;
MKVLLSGTAG PYGWPEPTCG CASCGRLPAG HRLPTAVVLD DVLRLAPPAG LPVTPPATLP
KGYRMTVTPD GYAVSGPDRG RVLHAVPPGE RGGTPSPCWA EDDYDLVLID LLDRPQRLGD
LRRRGLVTAR TRVVAVNLDH RVPSEAELGR RLAFWGAEVV DDGTILDTRQ PVPARPPAPK
RVLLLGGARS GKSAEAELRL ITEPDVTYVA TGPTGRLDAD WLARVRAHQR RRPPYWTTIE
TTELEALLRS EAGPLLIDGI GTWLASVFDA CGAWDDPAHD RPRGRNPGRF GTALDAVAAR
CDDLVAAWRQ TRAQVVAVSD EVGLSVVPAT ASGRVFRDAL GRLNQGLAAE SEEATLVVAG
RVVPLPI
//
