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Database: UniProt
Entry: D3SL45_THEAH
LinkDB: D3SL45_THEAH
Original site: D3SL45_THEAH 
ID   D3SL45_THEAH            Unreviewed;       402 AA.
AC   D3SL45;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   OrderedLocusNames=Thal_0842 {ECO:0000313|EMBL:ADC89475.1};
OS   Thermocrinis albus (strain DSM 14484 / JCM 11386 / HI 11/12).
OC   Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Thermocrinis.
OX   NCBI_TaxID=638303 {ECO:0000313|EMBL:ADC89475.1, ECO:0000313|Proteomes:UP000002043};
RN   [1] {ECO:0000313|Proteomes:UP000002043}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14484 / JCM 11386 / HI 11/12
RC   {ECO:0000313|Proteomes:UP000002043};
RX   DOI=10.4056/sigs.761490;
RA   Wirth R., Sikorski J., Brambilla E., Misra M., Lapidus A., Copeland A.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Han C., Detter J.C.,
RA   Tapia R., Bruce D., Goodwin L., Pitluck S., Pati A., Anderson I.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Chen A., Palaniappan K.,
RA   Bilek Y., Hader T., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Tindall B.J., Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Thermocrinis albus type strain (HI 11/12T).";
RL   Stand. Genomic Sci. 2:194-202(2010).
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; CP001931; ADC89475.1; -; Genomic_DNA.
DR   RefSeq; WP_012991881.1; NC_013894.1.
DR   AlphaFoldDB; D3SL45; -.
DR   STRING; 638303.Thal_0842; -.
DR   KEGG; tal:Thal_0842; -.
DR   eggNOG; COG0303; Bacteria.
DR   HOGENOM; CLU_010186_7_2_0; -.
DR   OMA; MTGAMVP; -.
DR   OrthoDB; 9804758at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000002043; 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; 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.
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:UP000002043};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          179..317
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   402 AA;  44234 MW;  E9BB2D2158EAF90C CRC64;
     MISYQEALRI LLENTQPLGT ERVFLKDAVG RVLASSVVSP EDRPSFDNSA MDGYAVISED
     TEGASEDSPV LLKLVGEVPA GVWPSCKVEK KTAVKIFTGA PLPEGADAVV PVEYTQEKDG
     YVVVKKRVPA GANVRRKGEE FRRGEILLEE GTTLRHYEIA LLASINVVQV EVYRRPRVGI
     LSTGDELVDL GEEITSPSQI RTSNNYGLLA GVILAGGEPH LLGIVGDEPV KLGKLMKSIE
     EYDVFITTGG VSVGERDLVK VLVEEYGVDV KFHKVRIKPA KPVLFGLKGK TLFFGLPGNP
     VSTMIAFDLL VKPALLKLQG VRNHVPQIQK ATLVRDFSRK DSERLEFVRA RVWWEGDTFL
     CDYSPKTQSH MLTSYVGMNA YMIVPEGVNT LREGDRVDVI LL
//
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