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Database: UniProt
Entry: A0A2U0SI59_9SPHN
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ID   A0A2U0SI59_9SPHN        Unreviewed;       168 AA.
AC   A0A2U0SI59;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
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   ORFNames=DD559_18210 {ECO:0000313|EMBL:PVX31026.1};
OS   Sphingomonas pokkalii.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=2175090 {ECO:0000313|EMBL:PVX31026.1, ECO:0000313|Proteomes:UP000245890};
RN   [1] {ECO:0000313|EMBL:PVX31026.1, ECO:0000313|Proteomes:UP000245890}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L3B27 {ECO:0000313|EMBL:PVX31026.1,
RC   ECO:0000313|Proteomes:UP000245890};
RA   Menon R., Kumari S., Rameshkumar N.;
RT   "Description of Sphingomonas pokkalii sp nov, isolated from the rhizosphere
RT   of saline tolerant pokkali rice and its draft genome analysis.";
RL   Submitted (MAY-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, 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:PVX31026.1}.
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DR   EMBL; QENQ01000001; PVX31026.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U0SI59; -.
DR   OrthoDB; 9788370at2; -.
DR   UniPathway; UPA00148; UER00236.
DR   Proteomes; UP000245890; 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|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR006135};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR006135};
KW   Nucleotidyltransferase {ECO:0000313|EMBL:PVX31026.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006135}.
FT   ACT_SITE        49
FT                   /note="GMP-histidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006135-1"
FT   BINDING         8..15
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006135-2"
FT   BINDING         33..35
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006135-2"
FT   BINDING         50..53
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006135-2"
FT   BINDING         61
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006135-2"
FT   BINDING         83
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006135-2"
SQ   SEQUENCE   168 AA;  17853 MW;  0CC09B92E03FB06D CRC64;
     MTKLLVLGGA RSGKSRYAQA RAEFLPGTLL YVATAQALDG EMADRIARHR DDRGPRWSTL
     EVPIDLSAAI AANAAPDRVL LIDCLTLWTS NLLFAKRDLD AETEALAVAL AQATGPVVLV
     ANEVGLGIVP DNALARRFRD AAGRLNQAVA AVAQEVQFVA AGLPLRLK
//
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