GenomeNet

Database: UniProt
Entry: D0LAJ1_GORB4
LinkDB: D0LAJ1_GORB4
Original site: D0LAJ1_GORB4 
ID   D0LAJ1_GORB4            Unreviewed;       206 AA.
AC   D0LAJ1;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=Probable molybdenum cofactor guanylyltransferase {ECO:0000256|HAMAP-Rule:MF_00316};
DE            Short=MoCo guanylyltransferase {ECO:0000256|HAMAP-Rule:MF_00316};
DE            EC=2.7.7.77 {ECO:0000256|HAMAP-Rule:MF_00316};
DE   AltName: Full=GTP:molybdopterin guanylyltransferase {ECO:0000256|HAMAP-Rule:MF_00316};
DE   AltName: Full=Mo-MPT guanylyltransferase {ECO:0000256|HAMAP-Rule:MF_00316};
DE   AltName: Full=Molybdopterin guanylyltransferase {ECO:0000256|HAMAP-Rule:MF_00316};
DE   AltName: Full=Molybdopterin-guanine dinucleotide synthase {ECO:0000256|HAMAP-Rule:MF_00316};
DE            Short=MGD synthase {ECO:0000256|HAMAP-Rule:MF_00316};
GN   Name=mobA {ECO:0000256|HAMAP-Rule:MF_00316};
GN   OrderedLocusNames=Gbro_2052 {ECO:0000313|EMBL:ACY21304.1};
OS   Gordonia bronchialis (strain ATCC 25592 / DSM 43247 / BCRC 13721 / JCM 3198
OS   / KCTC 3076 / NBRC 16047 / NCTC 10667) (Rhodococcus bronchialis).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=526226 {ECO:0000313|EMBL:ACY21304.1, ECO:0000313|Proteomes:UP000001219};
RN   [1] {ECO:0000313|Proteomes:UP000001219}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25592 / DSM 43247 / BCRC 13721 / JCM 3198 / KCTC 3076 /
RC   NBRC 16047 / NCTC 10667 {ECO:0000313|Proteomes:UP000001219};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Ovchinnikova G., Saunders E., Brettin T., Detter J.C., Han C., Larimer F.,
RA   Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T.,
RA   Wu D., Jando M., Schneider S., Goeker M., Klenk H.-P., Eisen J.A.;
RT   "The complete chromosome of Gordonia bronchialis DSM 43247.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACY21304.1, ECO:0000313|Proteomes:UP000001219}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25592 / DSM 43247 / BCRC 13721 / JCM 3198 / KCTC 3076 /
RC   NBRC 16047 / NCTC 10667 {ECO:0000313|Proteomes:UP000001219};
RX   PubMed=21304674;
RA   Ivanova N., Sikorski J., Jando M., Lapidus A., Nolan M., Lucas S.,
RA   Del Rio T.G., Tice H., Copeland A., Cheng J.F., Chen F., Bruce D.,
RA   Goodwin L., Pitluck S., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P.,
RA   Saunders E., Han C., Detter J.C., Brettin T., Rohde M., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P.,
RA   Kyrpides N.C.;
RT   "Complete genome sequence of Gordonia bronchialis type strain (3410).";
RL   Stand. Genomic Sci. 2:19-28(2010).
CC   -!- FUNCTION: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT)
CC       cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine
CC       dinucleotide (Mo-MGD) cofactor. {ECO:0000256|HAMAP-Rule:MF_00316}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin
CC         guanine dinucleotide; Xref=Rhea:RHEA:34243, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:71302,
CC         ChEBI:CHEBI:71310; EC=2.7.7.77; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00316};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00316};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00316}.
CC   -!- DOMAIN: The N-terminal domain determines nucleotide recognition and
CC       specific binding, while the C-terminal domain determines the specific
CC       binding to the target protein. {ECO:0000256|HAMAP-Rule:MF_00316}.
CC   -!- SIMILARITY: Belongs to the MobA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00316}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00316}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001802; ACY21304.1; -; Genomic_DNA.
DR   RefSeq; WP_012833862.1; NC_013441.1.
DR   AlphaFoldDB; D0LAJ1; -.
DR   STRING; 526226.Gbro_2052; -.
DR   KEGG; gbr:Gbro_2052; -.
DR   eggNOG; COG0746; Bacteria.
DR   HOGENOM; CLU_055597_3_2_11; -.
DR   OrthoDB; 9788394at2; -.
DR   Proteomes; UP000001219; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061603; F:molybdenum cofactor guanylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd02503; MobA; 1.
DR   HAMAP; MF_00316; MobA; 1.
DR   InterPro; IPR025877; MobA-like_NTP_Trfase.
DR   InterPro; IPR013482; Molybde_CF_guanTrfase.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR19136; MOLYBDENUM COFACTOR GUANYLYLTRANSFERASE; 1.
DR   PANTHER; PTHR19136:SF81; MOLYBDENUM COFACTOR GUANYLYLTRANSFERASE; 1.
DR   Pfam; PF12804; NTP_transf_3; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00316};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_00316}; Magnesium {ECO:0000256|HAMAP-Rule:MF_00316};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00316};
KW   Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150,
KW   ECO:0000256|HAMAP-Rule:MF_00316};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00316}; Reference proteome {ECO:0000313|Proteomes:UP000001219};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00316}.
FT   DOMAIN          16..176
FT                   /note="MobA-like NTP transferase"
FT                   /evidence="ECO:0000259|Pfam:PF12804"
FT   BINDING         19..21
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00316"
FT   BINDING         31
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00316"
FT   BINDING         83
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00316"
FT   BINDING         115
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00316"
FT   BINDING         115
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00316"
SQ   SEQUENCE   206 AA;  21539 MW;  D01A5B0661008141 CRC64;
     MADQEQNRAS DGRLAGIVLA GGRSRRMGQD KAALDWDGEP MLARIVRVAA QRCEPILVVA
     AESSSAYQGL FGTGGPQAQW ITDEEPGAGP LGGLVAGLRA AAAGGAELAF VCATDMPLIS
     AELIDELLRG VTPSAQAVIA HDSQRDHPMA GIYRTAAAEV IAGVVATGER RMTAALDALT
     THRVAVSEPD WLVNVNAPED LHRLRV
//
DBGET integrated database retrieval system