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
//