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Database: UniProt
Entry: Q5FTR6_GLUOX
LinkDB: Q5FTR6_GLUOX
Original site: Q5FTR6_GLUOX 
ID   Q5FTR6_GLUOX            Unreviewed;       398 AA.
AC   Q5FTR6;
DT   01-MAR-2005, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2005, sequence version 1.
DT   24-JAN-2024, entry version 92.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   OrderedLocusNames=GOX0447 {ECO:0000313|EMBL:AAW60230.1};
OS   Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconobacter.
OX   NCBI_TaxID=290633 {ECO:0000313|EMBL:AAW60230.1, ECO:0000313|Proteomes:UP000006375};
RN   [1] {ECO:0000313|EMBL:AAW60230.1, ECO:0000313|Proteomes:UP000006375}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=621H {ECO:0000313|EMBL:AAW60230.1,
RC   ECO:0000313|Proteomes:UP000006375};
RX   PubMed=15665824; DOI=10.1038/nbt1062;
RA   Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA   Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT   "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT   oxydans.";
RL   Nat. Biotechnol. 23:195-200(2005).
CC   -!- FUNCTION: Catalyzes the insertion of molybdate into adenylated
CC       molybdopterin with the concomitant release of AMP.
CC       {ECO:0000256|ARBA:ARBA00002901, ECO:0000256|RuleBase:RU365090}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-
CC         molybdopterin; Xref=Rhea:RHEA:35047, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:36264, ChEBI:CHEBI:62727,
CC         ChEBI:CHEBI:71302, ChEBI:CHEBI:456215; EC=2.10.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001529};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU365090};
CC   -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005046, ECO:0000256|RuleBase:RU365090}.
CC   -!- SIMILARITY: Belongs to the MoeA family. {ECO:0000256|ARBA:ARBA00010763,
CC       ECO:0000256|RuleBase:RU365090}.
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DR   EMBL; CP000009; AAW60230.1; -; Genomic_DNA.
DR   RefSeq; WP_011252031.1; NZ_LT900338.1.
DR   AlphaFoldDB; Q5FTR6; -.
DR   STRING; 290633.GOX0447; -.
DR   KEGG; gox:GOX0447; -.
DR   eggNOG; COG0303; Bacteria.
DR   HOGENOM; CLU_010186_7_0_5; -.
DR   OMA; MTGAMVP; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000006375; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0061599; F:molybdopterin molybdotransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00887; MoeA; 1.
DR   Gene3D; 3.40.980.10; MoaB/Mog-like domain; 1.
DR   Gene3D; 2.40.340.10; MoeA, C-terminal, domain IV; 1.
DR   Gene3D; 3.90.105.10; Molybdopterin biosynthesis moea protein, domain 2; 1.
DR   Gene3D; 2.170.190.11; Molybdopterin biosynthesis moea protein, domain 3; 1.
DR   InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR   InterPro; IPR001453; MoaB/Mog_dom.
DR   InterPro; IPR008284; MoCF_biosynth_CS.
DR   InterPro; IPR038987; MoeA-like.
DR   InterPro; IPR005111; MoeA_C_domain_IV.
DR   InterPro; IPR036688; MoeA_C_domain_IV_sf.
DR   InterPro; IPR005110; MoeA_linker/N.
DR   InterPro; IPR036135; MoeA_linker/N_sf.
DR   NCBIfam; TIGR00177; molyb_syn; 1.
DR   PANTHER; PTHR10192:SF5; GEPHYRIN; 1.
DR   PANTHER; PTHR10192; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 1.
DR   Pfam; PF00994; MoCF_biosynth; 1.
DR   Pfam; PF03454; MoeA_C; 1.
DR   Pfam; PF03453; MoeA_N; 1.
DR   SMART; SM00852; MoCF_biosynth; 1.
DR   SUPFAM; SSF63867; MoeA C-terminal domain-like; 1.
DR   SUPFAM; SSF63882; MoeA N-terminal region -like; 1.
DR   SUPFAM; SSF53218; Molybdenum cofactor biosynthesis proteins; 1.
DR   PROSITE; PS01079; MOCF_BIOSYNTHESIS_2; 1.
PE   3: Inferred from homology;
KW   Magnesium {ECO:0000256|RuleBase:RU365090};
KW   Metal-binding {ECO:0000256|RuleBase:RU365090};
KW   Molybdenum {ECO:0000256|RuleBase:RU365090};
KW   Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150,
KW   ECO:0000256|RuleBase:RU365090};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006375};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          176..315
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   398 AA;  42629 MW;  DDE7FC2B037D9E2E CRC64;
     MSELLSVTRA MELVLDYAGS FGTETVDLTM AAGRILQQTI RAERAQPPYD RVMMDGIAFR
     HGSGPTLVSH GIQRAGAPGQ PLPEGHVCLE VMTGAVLPEG ADTVVPVERL VREGRLIRFE
     EGYEPRKGQF IHRRGSDCAA GTELLAPGQR LDGPALAVLA GNGHAQVSVS RIPSIGIVAT
     GDELVDVSAP VRDWEIRRSN EYALTGALLS RGFNCIERSV VPDDLAETIV ALREQLSRHD
     VLILSGGVSM GAFDHVPKAL SKIGVERVFH KVAQRPGKPL WFGVGPEGQR VFGLPGNPVS
     ATTCGVRYVM PMLLAGQGLC RPEPYTVMLD AEADLIPTLT RFLPVKVRHD ATGQALATPC
     PMPTSGDFSF LASTDGFVEL PRGEGMAPRG TAAMFHGW
//
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