ID A3XPA5_LEEBM Unreviewed; 192 AA.
AC A3XPA5;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 70.
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 ORFNames=MED217_08755 {ECO:0000313|EMBL:EAQ48624.1};
OS Leeuwenhoekiella blandensis (strain CECT 7118 / CCUG 51940 / KCTC 22103 /
OS MED217) (Flavobacterium sp. (strain MED217)).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Leeuwenhoekiella.
OX NCBI_TaxID=398720 {ECO:0000313|EMBL:EAQ48624.1, ECO:0000313|Proteomes:UP000001601};
RN [1] {ECO:0000313|EMBL:EAQ48624.1, ECO:0000313|Proteomes:UP000001601}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MED217 {ECO:0000313|EMBL:EAQ48624.1,
RC ECO:0000313|Proteomes:UP000001601};
RX PubMed=17215843; DOI=10.1038/nature05381;
RA Gomez-Consarnau L., Gonzalez J.M., Coll-Llado M., Gourdon P., Pascher T.,
RA Neutze R., Pedros-Alio C., Pinhassi J.;
RT "Light stimulates growth of proteorhodopsin-containing marine
RT Flavobacteria.";
RL Nature 445:210-213(2007).
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 -!- 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:EAQ48624.1}.
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; AANC01000007; EAQ48624.1; -; Genomic_DNA.
DR RefSeq; WP_009780127.1; NZ_CH672395.1.
DR AlphaFoldDB; A3XPA5; -.
DR STRING; 398720.MED217_08755; -.
DR eggNOG; COG0746; Bacteria.
DR HOGENOM; CLU_055597_2_0_10; -.
DR OrthoDB; 9788394at2; -.
DR Proteomes; UP000001601; Unassembled WGS sequence.
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:UP000001601};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00316}.
FT DOMAIN 11..155
FT /note="MobA-like NTP transferase"
FT /evidence="ECO:0000259|Pfam:PF12804"
FT BINDING 14..16
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00316"
FT BINDING 26
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00316"
FT BINDING 70
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00316"
FT BINDING 99
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00316"
FT BINDING 99
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00316"
SQ SEQUENCE 192 AA; 21804 MW; 5A65011402DD5366 CRC64;
MTETLKNNIP AYILCGGRSL RMGQDKGLVT LQKGEFITHI ISTLKPITDS IVLITENEEY
SRFGLPVIQD VYPEKGPLGG IHAALQHTEE SQILVFSCDI PLLKSYVIRE LIRFKNSADI
VFAKTEKRWH PLIGIYPKGL LSEVEENLNQ NKLRLIDFIK EHKYKAVNFI DDAAFTNINT
PEILARVEKN LV
//
