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Database: UniProt
Entry: F7YW47_9THEM
LinkDB: F7YW47_9THEM
Original site: F7YW47_9THEM 
ID   F7YW47_9THEM            Unreviewed;       641 AA.
AC   F7YW47;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   ORFNames=Theth_0441 {ECO:0000313|EMBL:AEH50536.1};
OS   Pseudothermotoga thermarum DSM 5069.
OC   Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC   Pseudothermotoga.
OX   NCBI_TaxID=688269 {ECO:0000313|EMBL:AEH50536.1, ECO:0000313|Proteomes:UP000006804};
RN   [1] {ECO:0000313|EMBL:AEH50536.1, ECO:0000313|Proteomes:UP000006804}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5069 {ECO:0000313|EMBL:AEH50536.1,
RC   ECO:0000313|Proteomes:UP000006804};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Zeytun A., Brettin T., Detter J.C.,
RA   Tapia R., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA   Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M., Brambilla E.,
RA   Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Thermotoga thermarum DSM 5069.";
RL   Submitted (NOV-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|RuleBase:RU365090}.
CC   -!- SIMILARITY: Belongs to the MoeA family. {ECO:0000256|ARBA:ARBA00010763,
CC       ECO:0000256|RuleBase:RU365090}.
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DR   EMBL; CP002351; AEH50536.1; -; Genomic_DNA.
DR   RefSeq; WP_013931759.1; NC_015707.1.
DR   AlphaFoldDB; F7YW47; -.
DR   STRING; 688269.Theth_0441; -.
DR   KEGG; tta:Theth_0441; -.
DR   PATRIC; fig|688269.3.peg.451; -.
DR   eggNOG; COG0303; Bacteria.
DR   eggNOG; COG1910; Bacteria.
DR   HOGENOM; CLU_010186_3_0_0; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000006804; 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; 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; 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:UP000006804};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          176..317
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   641 AA;  71348 MW;  8D89E361A36A7E5F CRC64;
     MRKIYLHRLD LPEALDKYIK KLDETGFFKV ESEVIPTRLA LNRVLAGSVY ARKSVPMFIS
     AAMDGIAVQS QHTVGATKAN PKRLKKDQFV FINTGNPMPE GFDAVIMIED VNIVDEETVE
     IYESVPPYHN VRMIGEDVCE GDMIFTRYHL LKPQDLALLL AVGVFEVEVV KKMKACMIPT
     GTEIVEPEKI TNDLHIPETN SVIVKNFLSM LGVDVEVLPP VPDDPTIIKE IVQNIAHDFD
     MILLGAGSSA GTVDYSYQVA EDLAEVIVHG INIRPGKPTI LAVLKTNPGK PLIGLPGYPG
     SCYVILEEIV KPIVLRKYKL ILPKSERIYA VSTRRISSSI SDDEIIRVSV GKVLDKYFFI
     PLKRGAAVME PLTKMDGKVV IPRGVEIVEE GELCQVETSK SLEEIDKNIL FVGSNDPIIS
     ILADFVKKYD YTIGMSISNV GSMGGLAAIA KKQAHIAGIH LLDAESGEYN IPYLKKYLEN
     FVLMKFVKRS QGLIVQKGNP KNIKSLLDLT KKGVRFVNRQ KASGTRILLD YHLQKLGIDP
     SHIEGYQDEE FTHLGVALKV KNGFADVGLG IALAAEIFNL DFIPLFWEEY DLLFLPEFLH
     DERFQLLLDV ISSKDFLDFA SKLKGYDLGQ ISKIIKSGDL T
//
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