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Database: UniProt
Entry: A5UEW5_HAEIG
LinkDB: A5UEW5_HAEIG
Original site: A5UEW5_HAEIG 
ID   A5UEW5_HAEIG            Unreviewed;       404 AA.
AC   A5UEW5;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   24-JAN-2024, entry version 74.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   Name=folE {ECO:0000313|EMBL:ABQ99320.1};
GN   OrderedLocusNames=CGSHiGG_01125 {ECO:0000313|EMBL:ABQ99320.1};
OS   Haemophilus influenzae (strain PittGG).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=374931 {ECO:0000313|EMBL:ABQ99320.1, ECO:0000313|Proteomes:UP000001990};
RN   [1] {ECO:0000313|EMBL:ABQ99320.1, ECO:0000313|Proteomes:UP000001990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PittGG {ECO:0000313|EMBL:ABQ99320.1,
RC   ECO:0000313|Proteomes:UP000001990};
RX   PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA   Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C.,
RA   Ehrlich G.D.;
RT   "Characterization and modeling of the Haemophilus influenzae core and
RT   supragenomes based on the complete genomic sequences of Rd and 12 clinical
RT   nontypeable strains.";
RL   Genome Biol. 8:R103.1-R103.18(2007).
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; CP000672; ABQ99320.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5UEW5; -.
DR   KEGG; hiq:CGSHiGG_01125; -.
DR   HOGENOM; CLU_010186_7_0_6; -.
DR   OMA; MTGAMVP; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000001990; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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   Hydrolase {ECO:0000313|EMBL:ABQ99320.1};
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   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          176..313
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   404 AA;  44195 MW;  5E2ADC416E54CC14 CRC64;
     MLTLDQARSK MLEQIPFPTQ TEYLNLKEAA NRICAEDIIS PINVPSFDNS AMDGYAVRLS
     DLQQSLTLSV AGKSFAGNPF QGEWPSKSAV RIMTGAMIPE GADAVIMQEQ VTLNEDGTVT
     FSELPKPNQN IRRIGEDVKK GDVVLEQGAP LTPVSLPLLA SLGIAEVKCY RQLKVGVLST
     GDELVEVGKP LQSGQIYDTN RFTVKLLLEK LHCEVIDLGL LPDNEAEFEK AFIAAQSQAD
     LVITSGGVSV GEADFTKAVL EKVGKVNFWK IAIKPGKPFA FGKLENAWFC GLPGNPVSAL
     ITFYQLVQPL IAKLQGQKQW KKPPHFSAIA TMNLKKAVGR LDFQRGFYYI NEQGQMEVQS
     VGFQGSHLFS AFVKSNCFIV LEQERGNVSA GETVTIEPFN HLLG
//
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