ID A0A372FYT3_9ACTN Unreviewed; 641 AA.
AC A0A372FYT3;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Adenosylcobinamide kinase {ECO:0000256|ARBA:ARBA00029570};
DE EC=2.7.1.156 {ECO:0000256|ARBA:ARBA00012016};
DE EC=2.7.7.62 {ECO:0000256|ARBA:ARBA00012523};
DE AltName: Full=Adenosylcobinamide-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00030571};
GN ORFNames=D0Q02_13825 {ECO:0000313|EMBL:RFS45945.1};
OS Micromonospora craniellae.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=2294034 {ECO:0000313|EMBL:RFS45945.1, ECO:0000313|Proteomes:UP000262621};
RN [1] {ECO:0000313|EMBL:RFS45945.1, ECO:0000313|Proteomes:UP000262621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LHW63014 {ECO:0000313|EMBL:RFS45945.1,
RC ECO:0000313|Proteomes:UP000262621};
RA Li L., Lin H.W.;
RT "Verrucosispora craniellae sp. nov., isolated from a marine sponge in the
RT South China Sea.";
RL Submitted (AUG-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}.
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 -!- 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 -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC adenosylcobalamin from cob(II)yrinate a,c-diamide: step 5/7.
CC {ECO:0000256|ARBA:ARBA00005159}.
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC adenosylcobalamin from cob(II)yrinate a,c-diamide: step 6/7.
CC {ECO:0000256|ARBA:ARBA00004692}.
CC -!- SIMILARITY: Belongs to the CobU/CobP family.
CC {ECO:0000256|ARBA:ARBA00007490}.
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:RFS45945.1}.
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DR EMBL; QVFU01000012; RFS45945.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A372FYT3; -.
DR OrthoDB; 9781491at2; -.
DR UniPathway; UPA00148; UER00236.
DR Proteomes; UP000262621; 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-KW.
DR GO; GO:0008820; F:cobinamide phosphate guanylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008939; F:nicotinate-nucleotide-dimethylbenzimidazole phosphoribosyltransferase activity; IEA:InterPro.
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; 3.40.50.10210; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003203; CobU/CobP.
DR InterPro; IPR003200; Nict_dMeBzImd_PRibTrfase.
DR InterPro; IPR036087; Nict_dMeBzImd_PRibTrfase_sf.
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 Pfam; PF02277; DBI_PRT; 1.
DR SUPFAM; SSF52733; Nicotinate mononucleotide:5,6-dimethylbenzimidazole phosphoribosyltransferase (CobT); 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000313|EMBL:RFS45945.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000313|EMBL:RFS45945.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000262621};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RFS45945.1}.
FT REGION 179..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 641 AA; 64582 MW; 8BB52CC7A82FBA7B CRC64;
MSLDGWNTLL VLGGIRSGKS EFAESLVADA ATVRYVATAA GGGDDDAEWA ARIAAHRERR
PATWNTEETA DDPRRLADVI AAARPEETLL VDDLGGWVTV LLDPAHQPAD DTVTVAELAA
AVRDCPARLV LVSPEVGLSL VPTTPLGRAF TDALGAVNRA VADACDAVVL VVAGQPVRLK
PATPEPAPAA EPSPGRSPVN GTAVPAQAGP SDARPADDAA ALPASPPVTT PEVPAAAAPV
PAADGTGRTP PAMTLPVADT GLVIQPGMEL PMPDDHTGPQ AVERLATLDV PGTGLGVLEQ
VVSFAAATQG TPTPIPWQSV RVLLLHGDHD GGSAAGTPDG ESARRAESAR AGQGVLARLA
AESGASLQVV TAPTAAAIED GPALTAEQVD AALRYGWRLA AEAVDSGVHL LVVAACGAGT
EAAAAAVLAA TAGAEAPAVL GRVVTPDGEI DDVAWMARCA AVRDALHRTR RASRDAKDVL
AQLGGGDIAV ATGILLGATA RRTPVLLDGP VGVAAGLVSR DLAGQARHWC MLADHGGHPA
VKLAADVLGL SPLTELRLDL GEGANALTVL PLLRSVLALA AALPPRPSGE AADDADEPEP
VEQDEPDFRE PEPAGPGPTS TETEPPGPTS TEPAEPGARA G
//