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Database: UniProt
Entry: C4GBH6_9FIRM
LinkDB: C4GBH6_9FIRM
Original site: C4GBH6_9FIRM 
ID   C4GBH6_9FIRM            Unreviewed;       206 AA.
AC   C4GBH6;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 46.
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=GCWU000342_01277 {ECO:0000313|EMBL:EEP28469.1};
OS   Shuttleworthia satelles DSM 14600.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Shuttleworthia.
OX   NCBI_TaxID=626523 {ECO:0000313|EMBL:EEP28469.1, ECO:0000313|Proteomes:UP000003494};
RN   [1] {ECO:0000313|EMBL:EEP28469.1, ECO:0000313|Proteomes:UP000003494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14600 {ECO:0000313|EMBL:EEP28469.1,
RC   ECO:0000313|Proteomes:UP000003494};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (APR-2009) 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:EEP28469.1}.
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DR   EMBL; ACIP02000002; EEP28469.1; -; Genomic_DNA.
DR   RefSeq; WP_006906287.1; NZ_GG665866.1.
DR   AlphaFoldDB; C4GBH6; -.
DR   STRING; 626523.GCWU000342_01277; -.
DR   eggNOG; COG2087; Bacteria.
DR   HOGENOM; CLU_094161_1_1_9; -.
DR   UniPathway; UPA00148; UER00236.
DR   Proteomes; UP000003494; Unassembled WGS sequence.
DR   GO; GO:0043752; F:adenosylcobinamide kinase activity; IEA:UniProtKB-EC.
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:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003494};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ   SEQUENCE   206 AA;  22965 MW;  BB62B1E3FE4F8824 CRC64;
     MMHLILGGSA SGKSEYAEKE ALRLAANQPL LYLATMKGDD PETLVRIDRH VRRRRGMGFV
     SLEIPYNLDC DRVKECLLTG LISDPAKGEA EAGDRLKRGK ALHLQTFSAK GVILLDCVSN
     LLANQIFDRH AMAYDPDRFC EGILSLREIC KDLLIVSNNV HEDGICYDEV TQDYIAQLGL
     INRRLGRASD RVTEVLAGLP VLLKER
//
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