ID Q47XZ5_COLP3 Unreviewed; 186 AA.
AC Q47XZ5;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=Bifunctional adenosylcobalamin biosynthesis protein {ECO:0000256|PIRNR:PIRNR006135};
DE EC=2.7.1.156 {ECO:0000256|PIRNR:PIRNR006135};
DE EC=2.7.7.62 {ECO:0000256|PIRNR:PIRNR006135};
GN Name=cobP {ECO:0000313|EMBL:AAZ24271.1};
GN OrderedLocusNames=CPS_3657 {ECO:0000313|EMBL:AAZ24271.1};
OS Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS psychroerythus).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Colwellia.
OX NCBI_TaxID=167879 {ECO:0000313|EMBL:AAZ24271.1, ECO:0000313|Proteomes:UP000000547};
RN [1] {ECO:0000313|EMBL:AAZ24271.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=34H {ECO:0000313|EMBL:AAZ24271.1};
RX PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT "The psychrophilic lifestyle as revealed by the genome sequence of
RT Colwellia psychrerythraea 34H through genomic and proteomic analyses.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005).
CC -!- FUNCTION: Catalyzes ATP-dependent phosphorylation of adenosylcobinamide
CC and addition of GMP to adenosylcobinamide phosphate.
CC {ECO:0000256|ARBA:ARBA00003889, ECO:0000256|PIRNR:PIRNR006135}.
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 ECO:0000256|PIRNR:PIRNR006135};
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 ECO:0000256|PIRNR:PIRNR006135};
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC adenosylcobalamin from cob(II)yrinate a,c-diamide: step 5/7.
CC {ECO:0000256|ARBA:ARBA00005159, ECO:0000256|PIRNR:PIRNR006135}.
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC adenosylcobalamin from cob(II)yrinate a,c-diamide: step 6/7.
CC {ECO:0000256|ARBA:ARBA00004692, ECO:0000256|PIRNR:PIRNR006135}.
CC -!- SIMILARITY: Belongs to the CobU/CobP family.
CC {ECO:0000256|ARBA:ARBA00007490, ECO:0000256|PIRNR:PIRNR006135}.
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; CP000083; AAZ24271.1; -; Genomic_DNA.
DR RefSeq; WP_011044411.1; NC_003910.7.
DR AlphaFoldDB; Q47XZ5; -.
DR STRING; 167879.CPS_3657; -.
DR KEGG; cps:CPS_3657; -.
DR HOGENOM; CLU_094161_0_1_6; -.
DR UniPathway; UPA00148; UER00236.
DR Proteomes; UP000000547; 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-UniRule.
DR GO; GO:0008820; F:cobinamide phosphate guanylyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniRule.
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 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, ECO:0000256|PIRNR:PIRNR006135};
KW Cobalamin biosynthesis {ECO:0000256|PIRNR:PIRNR006135};
KW GTP-binding {ECO:0000256|PIRNR:PIRNR006135, ECO:0000256|PIRSR:PIRSR006135-
KW 2}; Kinase {ECO:0000256|PIRNR:PIRNR006135};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR006135};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006135}.
FT ACT_SITE 52
FT /note="GMP-histidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006135-1"
FT BINDING 7..14
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR006135-2"
FT BINDING 36..38
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 88
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR006135-2"
SQ SEQUENCE 186 AA; 20378 MW; 81636D31E24261B5 CRC64;
MIHLVLGGAR SGKSRFAEQQ TLELSVKQGK QAVYIATATA IDPEMDNRIA QHQSDRGARG
ESWQLIECPL ALAETLSDLD NNNVYLLDCL TLWLNNQLYA VHEENRGQQS QHLQTEIDKL
ATGLASVNAD IIIVSNEIGL GVIPMGESTR LYVDYCGWLN QKVAEVSDKV TLVTAGIPLC
IKSNGE
//
