COBY_METJA
ID COBY_METJA Reviewed; 196 AA.
AC Q58517;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Adenosylcobinamide-phosphate guanylyltransferase;
DE Short=AdoCbi-P guanylyltransferase;
DE EC=2.7.7.62;
GN Name=cobY; OrderedLocusNames=MJ1117;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION AS A NUCLEOTIDYLTRANSFERASE, AND KINETIC PARAMETERS.
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=18260642; DOI=10.1021/bi702475t;
RA Grochowski L.L., Xu H., White R.H.;
RT "Identification and characterization of the 2-phospho-L-lactate
RT guanylyltransferase involved in coenzyme F420 biosynthesis.";
RL Biochemistry 47:3033-3037(2008).
RN [3]
RP FUNCTION IN ADENOSYLCOBALAMIN BIOSYNTHESIS, CATALYTIC ACTIVITY,
RP GTP-BINDING, SUBSTRATE SPECIFICITY, SUBUNIT, ORDER OF SUBSTRATE BINDING,
RP AND KINETIC PARAMETERS.
RX PubMed=19489548; DOI=10.1021/bi8023114;
RA Otte M.M., Escalante-Semerena J.C.;
RT "Biochemical characterization of the GTP:adenosylcobinamide-phosphate
RT guanylyltransferase (CobY) enzyme of the hyperthermophilic archaeon
RT Methanocaldococcus jannaschii.";
RL Biochemistry 48:5882-5889(2009).
CC -!- FUNCTION: Guanylyltransferase that catalyzes the synthesis of
CC adenosylcobinamide-GDP (AdoCbi-GDP) from adenosylcobinamide-phosphate
CC (AdoCbi-P) and GTP. Is involved in adenosylcobalamin biosynthesis.
CC Binds one GTP per dimer. Cannot use other NTPs or GDP. Does not display
CC AdoCbi kinase activity. Is also able to catalyze the condensation of 2-
CC phospho-L-lactate (LP) with GTP in vitro to form PPi and (2S)-lactyl-2-
CC diphospho-5'-guanosine (LPPG), but is much less efficient than CofC,
CC the presumed enzyme catalyzing this reaction in vivo.
CC {ECO:0000269|PubMed:18260642, ECO:0000269|PubMed:19489548}.
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:0000269|PubMed:19489548};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=18.4 uM for adenosylcobinamide phosphate
CC {ECO:0000269|PubMed:18260642, ECO:0000269|PubMed:19489548};
CC KM=2.4 uM for GTP {ECO:0000269|PubMed:18260642,
CC ECO:0000269|PubMed:19489548};
CC KM=6 mM for (2S)-2-phospholactate {ECO:0000269|PubMed:18260642,
CC ECO:0000269|PubMed:19489548};
CC Vmax=115 nmol/min/mg enzyme with (2S)-2-phospholactate as substrate
CC {ECO:0000269|PubMed:18260642, ECO:0000269|PubMed:19489548};
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19489548}.
CC -!- MISCELLANEOUS: Binds GTP first, before binding AdoCbi-P.
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DR EMBL; L77117; AAB99118.1; -; Genomic_DNA.
DR PIR; D64439; D64439.
DR RefSeq; WP_010870628.1; NC_000909.1.
DR PDB; 2MZB; NMR; -; A=1-196.
DR PDB; 3RSB; X-ray; 2.80 A; A/B/C/D=1-196.
DR PDBsum; 2MZB; -.
DR PDBsum; 3RSB; -.
DR AlphaFoldDB; Q58517; -.
DR BMRB; Q58517; -.
DR SMR; Q58517; -.
DR STRING; 243232.MJ_1117; -.
DR EnsemblBacteria; AAB99118; AAB99118; MJ_1117.
DR GeneID; 1452013; -.
DR KEGG; mja:MJ_1117; -.
DR eggNOG; arCOG01871; Archaea.
DR HOGENOM; CLU_098907_0_0_2; -.
DR InParanoid; Q58517; -.
DR OMA; GMGEKPC; -.
DR OrthoDB; 90478at2157; -.
DR PhylomeDB; Q58517; -.
DR BRENDA; 2.7.7.62; 3260.
DR SABIO-RK; Q58517; -.
DR UniPathway; UPA00148; -.
DR EvolutionaryTrace; Q58517; -.
DR PRO; PR:Q58517; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0008820; F:cobinamide phosphate guanylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IDA:UniProtKB.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR005245; CHP00454.
DR InterPro; IPR025877; MobA-like_NTP_Trfase.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF12804; NTP_transf_3; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR TIGRFAMs; TIGR00454; TIGR00454; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cobalamin biosynthesis; GTP-binding; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..196
FT /note="Adenosylcobinamide-phosphate guanylyltransferase"
FT /id="PRO_0000107174"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:3RSB"
FT HELIX 13..16
FT /evidence="ECO:0007829|PDB:3RSB"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:3RSB"
FT HELIX 29..38
FT /evidence="ECO:0007829|PDB:3RSB"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:3RSB"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:3RSB"
FT HELIX 54..63
FT /evidence="ECO:0007829|PDB:3RSB"
FT TURN 64..68
FT /evidence="ECO:0007829|PDB:3RSB"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:3RSB"
FT TURN 86..90
FT /evidence="ECO:0007829|PDB:3RSB"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:3RSB"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:3RSB"
FT HELIX 107..121
FT /evidence="ECO:0007829|PDB:3RSB"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:3RSB"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:3RSB"
FT STRAND 146..157
FT /evidence="ECO:0007829|PDB:3RSB"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:3RSB"
FT HELIX 181..189
FT /evidence="ECO:0007829|PDB:3RSB"
SQ SEQUENCE 196 AA; 21746 MW; 6E5F4F07A0F509D4 CRC64;
MDALIMAGGK GTRMGGVEKP LIKLCGRCLI DYVVSPLLKS KVNNIFIATS PNTPKTKEYI
NSAYKDYKNI VVIDTSGKGY IEDLNECIGY FSEPFLVVSS DLINLKSKII NSIVDYFYCI
KAKTPDVEAL AVMIPKEKYP NPSIDFNGLV PAGINVVSPK HGYQKEEIMV IDELIFNINT
KDDLKLAEML LKKDGL
