COBP_PSEAE
ID COBP_PSEAE Reviewed; 173 AA.
AC Q9I466;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 102.
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; OrderedLocusNames=PA1278;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
CC -!- FUNCTION: Catalyzes ATP-dependent phosphorylation of adenosylcobinamide
CC and addition of GMP to adenosylcobinamide phosphate. {ECO:0000250}.
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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CobU/CobP family. {ECO:0000305}.
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DR EMBL; AE004091; AAG04667.1; -; Genomic_DNA.
DR PIR; D83486; D83486.
DR RefSeq; NP_249969.1; NC_002516.2.
DR RefSeq; WP_003082599.1; NZ_QZGE01000005.1.
DR AlphaFoldDB; Q9I466; -.
DR SMR; Q9I466; -.
DR STRING; 287.DR97_657; -.
DR PaxDb; Q9I466; -.
DR PRIDE; Q9I466; -.
DR EnsemblBacteria; AAG04667; AAG04667; PA1278.
DR GeneID; 881443; -.
DR KEGG; pae:PA1278; -.
DR PATRIC; fig|208964.12.peg.1328; -.
DR PseudoCAP; PA1278; -.
DR HOGENOM; CLU_094161_0_1_6; -.
DR InParanoid; Q9I466; -.
DR OMA; DCLTVWL; -.
DR PhylomeDB; Q9I466; -.
DR BioCyc; PAER208964:G1FZ6-1303-MON; -.
DR UniPathway; UPA00148; UER00236.
DR UniPathway; UPA00148; UER00237.
DR Proteomes; UP000002438; 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; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW ATP-binding; Cobalamin biosynthesis; GTP-binding; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..173
FT /note="Bifunctional adenosylcobalamin biosynthesis protein
FT CobP"
FT /id="PRO_0000287789"
FT ACT_SITE 48
FT /note="GMP-histidine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 7..14
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 32..34
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 49..52
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 60
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 173 AA; 18862 MW; EE3DDDC3858CC8DF CRC64;
MRDLILGGAR SGKSRLAERL AAESGLAVSY IATAQAGDGE MGRRIAEHRA RRPAHWRTLE
EPLALAATLR SEAEAGRCLL VDCLTLWLTN LLLCDDPQRL DGEREALLEC LGELPGRIIL
VSNETGLGVV PLGELSRRYV DEAGWLHQAI AERCERVTFT VAGLPMPLKG EPL
