(data stored in ACNUC7421 zone)

SWISSPROT: MOBA_HISS2

ID   MOBA_HISS2              Reviewed;         195 AA.
AC   B0UVP3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   11-DEC-2019, entry version 63.
DE   RecName: Full=Molybdenum cofactor guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_00316};
DE            Short=MoCo guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_00316};
DE            EC=2.7.7.77 {ECO:0000255|HAMAP-Rule:MF_00316};
DE   AltName: Full=GTP:molybdopterin guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_00316};
DE   AltName: Full=Mo-MPT guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_00316};
DE   AltName: Full=Molybdopterin guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_00316};
DE   AltName: Full=Molybdopterin-guanine dinucleotide synthase {ECO:0000255|HAMAP-Rule:MF_00316};
DE            Short=MGD synthase {ECO:0000255|HAMAP-Rule:MF_00316};
GN   Name=mobA {ECO:0000255|HAMAP-Rule:MF_00316}; OrderedLocusNames=HSM_0182;
OS   Histophilus somni (strain 2336) (Haemophilus somnus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=228400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2336;
RG   US DOE Joint Genome Institute;
RA   Siddaramappa S., Duncan A.J., Challacombe J.F., Rainey D., Gillaspy A.F.,
RA   Carson M., Gipson J., Gipson M., Bruce D., Detter J.C., Han C.S., Land M.,
RA   Tapia R., Thompson L.S., Orvis J., Zaitshik J., Barnes G., Brettin T.S.,
RA   Dyer D.W., Inzana T.J.;
RT   "Complete sequence of Haemophilus somnus 2336.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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:0000255|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:0000255|HAMAP-
CC         Rule:MF_00316};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00316};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00316}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_00316}.
CC   -!- SIMILARITY: Belongs to the MobA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00316}.
DR   EMBL; CP000947; ACA31607.1; -; Genomic_DNA.
DR   RefSeq; WP_012340917.1; NC_010519.1.
DR   SMR; B0UVP3; -.
DR   EnsemblBacteria; ACA31607; ACA31607; HSM_0182.
DR   GeneID; 31486460; -.
DR   KEGG; hsm:HSM_0182; -.
DR   HOGENOM; HOG000280423; -.
DR   KO; K03752; -.
DR   OMA; FVPCDVP; -.
DR   OrthoDB; 2019898at2; -.
DR   BioCyc; HSOM228400:G1GB8-187-MONOMER; -.
DR   Proteomes; UP000008543; 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   Gene3D; 3.90.550.10; -; 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   Pfam; PF12804; NTP_transf_3; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   TIGRFAMs; TIGR02665; molyb_mobA; 1.
PE   3: Inferred from homology;
DR   PRODOM; B0UVP3.
DR   SWISS-2DPAGE; B0UVP3.
KW   Cytoplasm; GTP-binding; Magnesium; Metal-binding;
KW   Molybdenum cofactor biosynthesis; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..195
FT                   /note="Molybdenum cofactor guanylyltransferase"
FT                   /id="PRO_1000079109"
FT   NP_BIND         10..12
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00316"
FT   METAL           99
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00316"
FT   BINDING         23
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00316"
FT   BINDING         51
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00316"
FT   BINDING         69
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00316"
FT   BINDING         99
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00316"
SQ   SEQUENCE   195 AA;  21815 MW;  11B4F9A8D67C7733 CRC64;
     MATTISAVIL AGGQAKRMAG LDKGLQLLQG KPLYQHCLQR LTNQVSSISI NANRHQAIYQ
     QSGVEVFGDE LEDFQGPLSG ILTALERANT DFVLFVPCDS PFLPLNLCEK LQSAVENSKS
     LLAYANDGER EHPAFSLLST QLKLPLRVYL QSGHRQMLQF FRQHKAISVD FSLQKQAFVN
     MNTLQDIEKY QNIYA
//

If you have problems or comments...

PBIL Back to PBIL home page