COBP_SINSX
ID COBP_SINSX Reviewed; 174 AA.
AC P29931;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Bifunctional adenosylcobalamin biosynthesis protein CobP;
DE AltName: Full=Adenosylcobinamide kinase;
DE EC=2.7.1.156;
DE AltName: Full=Adenosylcobinamide-phosphate guanylyltransferase;
DE EC=2.7.7.62;
GN Name=cobP;
OS Sinorhizobium sp.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=42445;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SC510;
RX PubMed=1655697; DOI=10.1128/jb.173.19.6074-6087.1991;
RA Crouzet J., Levy-Schil S., Cameron B., Cauchois L., Rigault S.,
RA Rouyez M.-C., Blanche F., Debussche L., Thibaut D.;
RT "Nucleotide sequence and genetic analysis of a 13.1-kilobase-pair
RT Pseudomonas denitrificans DNA fragment containing five cob genes and
RT identification of structural genes encoding Cob(I)alamin
RT adenosyltransferase, cobyric acid synthase, and bifunctional cobinamide
RT kinase-cobinamide phosphate guanylyltransferase.";
RL J. Bacteriol. 173:6074-6087(1991).
RN [2]
RP CHARACTERIZATION, AND PROTEIN SEQUENCE OF 2-11.
RX PubMed=1655696; DOI=10.1128/jb.173.19.6052-6057.1991;
RA Blanche F., Debussche L., Famechon A., Thibaut D., Cameron B., Crouzet J.;
RT "A bifunctional protein from Pseudomonas denitrificans carries cobinamide
RT kinase and cobinamide phosphate guanylyltransferase activities.";
RL J. Bacteriol. 173:6052-6057(1991).
CC -!- FUNCTION: Catalyzes ATP-dependent phosphorylation of adenosylcobinamide
CC and addition of GMP to adenosylcobinamide phosphate.
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 -!- 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 -!- 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 -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC adenosylcobalamin from cob(II)yrinate a,c-diamide: step 5/7.
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC adenosylcobalamin from cob(II)yrinate a,c-diamide: step 6/7.
CC -!- SUBUNIT: Homodimer.
CC -!- SIMILARITY: Belongs to the CobU/CobP family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to originate from Pseudomonas
CC denitrificans, but similarity searches show that the sequence is much
CC closer to Sinorhizobium. The entry's taxonomy has been changed.
CC {ECO:0000305}.
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DR EMBL; M62866; AAA25778.1; -; Genomic_DNA.
DR AlphaFoldDB; P29931; -.
DR SMR; P29931; -.
DR BioCyc; MetaCyc:MON-143; -.
DR UniPathway; UPA00148; UER00236.
DR UniPathway; UPA00148; UER00237.
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; -; 1.
DR InterPro; IPR003203; Cobinamide_kinase/P_G-Trfase.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR34848; PTHR34848; 1.
DR Pfam; PF02283; CobU; 1.
DR PIRSF; PIRSF006135; CobU; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cobalamin biosynthesis; Direct protein sequencing;
KW GTP-binding; Kinase; Nucleotide-binding; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1655696"
FT CHAIN 2..174
FT /note="Bifunctional adenosylcobalamin biosynthesis protein
FT CobP"
FT /id="PRO_0000089993"
FT ACT_SITE 54
FT /note="GMP-histidine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 13..20
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 38..40
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 55..58
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 174 AA; 19442 MW; 71580200BC9DC4DC CRC64;
MSSLSAGPVL VLGGARSGKS SFSERLVEAS GFTMHYVATG RAWDDEMRER IDHHRTRRGE
GWTTHEEPLD LVGILRRIDD PSHVVLIDCL TLWVTNLMLE ERDMTAEFAA LVAYLPEARA
RLVFVSNEVG LGIVPENRMA REFRDHAGRL HQIVAEKSAE VYFVAAGLPL KMKG
