ID A0A2S4XUN5_9ACTN Unreviewed; 411 AA.
AC A0A2S4XUN5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-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=C3486_15225 {ECO:0000313|EMBL:POX40160.1};
OS Streptomyces sp. Ru73.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2080748 {ECO:0000313|EMBL:POX40160.1, ECO:0000313|Proteomes:UP000236956};
RN [1] {ECO:0000313|EMBL:POX40160.1, ECO:0000313|Proteomes:UP000236956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ru73 {ECO:0000313|EMBL:POX40160.1,
RC ECO:0000313|Proteomes:UP000236956};
RA Suneja G., Sharma R.;
RT "Genome sequencing of cellulose degrading bacteria.";
RL Submitted (FEB-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:POX40160.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PQSQ01000028; POX40160.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S4XUN5; -.
DR OrthoDB; 9788370at2; -.
DR UniPathway; UPA00148; UER00236.
DR Proteomes; UP000236956; 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 Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR InterPro; IPR003203; CobU/CobP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR PANTHER; PTHR34848; -; 1.
DR PANTHER; PTHR34848:SF1; BIFUNCTIONAL ADENOSYLCOBALAMIN BIOSYNTHESIS PROTEIN COBU; 1.
DR Pfam; PF02283; CobU; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 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:POX40160.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000236956};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:POX40160.1}.
SQ SEQUENCE 411 AA; 42582 MW; 617BC2B129FD42A9 CRC64;
MTLLGTGAPD GLPRPGCPCA SCAGATGDAA RAATALLLDG ALLLDLTPGA AFAAARAGQS
LTGVRQVLLT HPHEGPAVEV PTGLPQPGRV ADGRELALLD GHRVRAVAVD VPGTGYEIGG
PYGERLLYLP PGAAPAGASE GKGPYEMVVL DVLGRPDALA RLRANGAVDA ATDVIAVHIG
HDTPPGEELH RRLAAVGARA VPDGTSLLVG EYHAVPDLPR RTLVLGGARS GKSVEAERRL
AAFPDVLYVA TGGLRDGDTE WAARVTAHRE RRPASWRTAE TCDLVPLLAG EEEDGDGPGE
TEKTAASPLL IDCLSLWLTH AMDEVGAWDD ETWANGGERA LHARVDELVA AVRATRRPLV
AVSNEVGSGV VPATPAGRRF RDELGRLNAR FAAECEHVLL VVAGQALALR G
//
