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Database: UniProt
Entry: V4Y1W2_9PROT
LinkDB: V4Y1W2_9PROT
Original site: V4Y1W2_9PROT 
ID   V4Y1W2_9PROT            Unreviewed;       191 AA.
AC   V4Y1W2;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
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};
DE   Flags: Precursor;
GN   Name=cobP {ECO:0000313|EMBL:ESS14624.1};
GN   ORFNames=MOLA814_00183 {ECO:0000313|EMBL:ESS14624.1};
OS   Betaproteobacteria bacterium MOLA814.
OC   Bacteria; Pseudomonadota; Betaproteobacteria.
OX   NCBI_TaxID=1408164 {ECO:0000313|EMBL:ESS14624.1, ECO:0000313|Proteomes:UP000017838};
RN   [1] {ECO:0000313|EMBL:ESS14624.1, ECO:0000313|Proteomes:UP000017838}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MOLA814 {ECO:0000313|EMBL:ESS14624.1,
RC   ECO:0000313|Proteomes:UP000017838};
RX   PubMed=24356832;
RA   Courties A., Riedel T., Jarek M., Intertaglia L., Lebaron P., Suzuki M.T.;
RT   "Genome Sequence of Strain MOLA814, a Proteorhodopsin-Containing
RT   Representative of the Betaproteobacteria Common in the Ocean.";
RL   Genome Announc. 1:e01062-13(2013).
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   -!- 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:ESS14624.1}.
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DR   EMBL; AYMW01000001; ESS14624.1; -; Genomic_DNA.
DR   AlphaFoldDB; V4Y1W2; -.
DR   STRING; 1408164.MOLA814_00183; -.
DR   PATRIC; fig|1408164.3.peg.501; -.
DR   eggNOG; COG2087; Bacteria.
DR   OrthoDB; 9788370at2; -.
DR   UniPathway; UPA00148; UER00236.
DR   Proteomes; UP000017838; Unassembled WGS sequence.
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, ECO:0000313|EMBL:ESS14624.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR006135};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017838};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006135}.
FT   ACT_SITE        57
FT                   /note="GMP-histidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006135-1"
FT   BINDING         11..18
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006135-2"
FT   BINDING         41..43
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006135-2"
FT   BINDING         72
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006135-2"
FT   BINDING         94
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006135-2"
SQ   SEQUENCE   191 AA;  20394 MW;  D532BDD169482B8A CRC64;
     MHIADSELII GGQKSGKSRR AEQLARVWLD ASGDHTAVLI ATAQPWDEEM RQRIERHQTD
     RAERVPGMTT LEEPLALAGA IRRVSTPTTL VVVDCLTLWL TNLLMPAKSV GDQPTYTSDT
     LPVADLAAAI ALAPGPVILV GNEIGLGVIP MGREVRAFVD ALGLLNQQVA STCERVTLMA
     AGLPLTLKGL S
//
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