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Database: UniProt
Entry: E8N0R4_ANATU
LinkDB: E8N0R4_ANATU
Original site: E8N0R4_ANATU 
ID   E8N0R4_ANATU            Unreviewed;       666 AA.
AC   E8N0R4;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   OrderedLocusNames=ANT_04250 {ECO:0000313|EMBL:BAJ62459.1};
OS   Anaerolinea thermophila (strain DSM 14523 / JCM 11388 / NBRC 100420 /
OS   UNI-1).
OC   Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC   Anaerolinea.
OX   NCBI_TaxID=926569 {ECO:0000313|EMBL:BAJ62459.1, ECO:0000313|Proteomes:UP000008922};
RN   [1] {ECO:0000313|EMBL:BAJ62459.1, ECO:0000313|Proteomes:UP000008922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14523 / JCM 11388 / NBRC 100420 / UNI-1
RC   {ECO:0000313|Proteomes:UP000008922};
RA   Narita-Yamada S., Kishi E., Watanabe Y., Takasaki K., Ankai A., Oguchi A.,
RA   Fukui S., Takahashi M., Yashiro I., Hosoyama A., Sekiguchi Y., Hanada S.,
RA   Fujita N.;
RT   "Whole genome sequence of Anaerolinea thermophila UNI-1.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
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; AP012029; BAJ62459.1; -; Genomic_DNA.
DR   AlphaFoldDB; E8N0R4; -.
DR   STRING; 926569.ANT_04250; -.
DR   KEGG; atm:ANT_04250; -.
DR   eggNOG; COG0303; Bacteria.
DR   eggNOG; COG1910; Bacteria.
DR   HOGENOM; CLU_010186_3_0_0; -.
DR   InParanoid; E8N0R4; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000008922; 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   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 1.
DR   InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR   InterPro; IPR001453; MoaB/Mog_dom.
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   InterPro; IPR024370; PBP_domain.
DR   PANTHER; PTHR10192; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 1.
DR   PANTHER; PTHR10192:SF16; MOLYBDOPTERIN MOLYBDENUMTRANSFERASE; 1.
DR   Pfam; PF00994; MoCF_biosynth; 1.
DR   Pfam; PF03454; MoeA_C; 1.
DR   Pfam; PF03453; MoeA_N; 1.
DR   Pfam; PF12727; PBP_like; 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   SUPFAM; SSF53850; Periplasmic binding protein-like II; 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:UP000008922};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          200..342
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   666 AA;  71985 MW;  C01345D37A461F96 CRC64;
     MCHNPEWGGK TMSVYLHDIP LPEAQQRLIQ ALEEVGLESV LGVEEIPLDE RALGRVLAEP
     VWARLSSPHY HASAMDGFAL RAEATAGASP TRPVILQVGE QAVYVDTGDP LPDWANAVVP
     IENVEALDEQ DIPAADARHP LKIRLREALP PWTHVRPMGE DIVATELVLP AGHTLRAVDL
     GAIAASGHTH VRVSRPPRVA ILPTGTELVP VGQPVKRGDI IEYNSLVLAA QVRSWGGEAV
     RFPITPDDFE QICQRVQQAA DMTDLVLLNA GSSAGSEDFS ARAVERLGTL LVHGVAVRPG
     HPVIMGLIRR SQGGWTPIIG VPGYPVSAAL TGEIFVEPLL ARWLGRRPAE PLEIEAQITR
     KVTSPAGDDD YMRVVVGKVG NRVLAAPLSR GAGVITSLVR ADGIVILPRG VQGLEAGAPV
     RVRLYRSPAE VEQTIFAIGS HDLTLDLLAQ ALSAHQRRLV SANVGSLGGL VALRRGEAHL
     AGAHLLDPQT GEFNIPYIRQ YLPDTPVTLV EWVGRIQGLL VCKGNPLNIR GLEDLVRAGV
     RFINRQRGAG TRILLDYHLE RLGIDPAKIQ GYDQEEYTHL AVAAAVASGR ADCGLGVMAA
     AQALDLDFIP LFTERYQLVI PTVYYESDLL APLRVLMQDE NFRRSVQGLP GYTVENMGQV
     VAQLPQ
//
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