ID G7VA20_THELD Unreviewed; 638 AA.
AC G7VA20;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN OrderedLocusNames=Tlie_0987 {ECO:0000313|EMBL:AER66720.1};
OS Thermovirga lienii (strain ATCC BAA-1197 / DSM 17291 / Cas60314).
OC Bacteria; Synergistota; Synergistia; Synergistales; Thermovirgaceae;
OC Thermovirga.
OX NCBI_TaxID=580340 {ECO:0000313|EMBL:AER66720.1, ECO:0000313|Proteomes:UP000005868};
RN [1] {ECO:0000313|Proteomes:UP000005868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1197 / DSM 17291 / Cas60314
RC {ECO:0000313|Proteomes:UP000005868};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Saunders E.,
RA Kyrpides N., Mavromatis K., Ivanova N., Last F.I., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M., Brambilla E.-M.,
RA Klenk H.-P., Eisen J.A.;
RT "The complete genome of chromosome of Thermovirga lienii DSM 17291.";
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AER66720.1, ECO:0000313|Proteomes:UP000005868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1197 / DSM 17291 / Cas60314
RC {ECO:0000313|Proteomes:UP000005868};
RX PubMed=22768366; DOI=10.4056/sigs.2726028;
RA Goker M., Saunders E., Lapidus A., Nolan M., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Han C., Tapia R., Goodwin L.A., Pitluck S.,
RA Liolios K., Mavromatis K., Pagani I., Ivanova N., Mikhailova N., Pati A.,
RA Chen A., Palaniappan K., Land M., Chang Y.J., Jeffries C.D.,
RA Brambilla E.M., Rohde M., Spring S., Detter J.C., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Genome sequence of the moderately thermophilic, amino-acid-degrading and
RT sulfur-reducing bacterium Thermovirga lienii type strain (Cas60314(T)).";
RL Stand. Genomic Sci. 6:230-239(2012).
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; CP003096; AER66720.1; -; Genomic_DNA.
DR AlphaFoldDB; G7VA20; -.
DR STRING; 580340.Tlie_0987; -.
DR KEGG; tli:Tlie_0987; -.
DR eggNOG; COG0303; Bacteria.
DR eggNOG; COG1910; Bacteria.
DR HOGENOM; CLU_010186_3_0_0; -.
DR OrthoDB; 9804758at2; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000005868; 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:SF33; MOLYBDENUM COFACTOR BIOSYNTHESIS PROTEIN MOEA2; 1.
DR PANTHER; PTHR10192; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 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:UP000005868};
KW Transferase {ECO:0000256|RuleBase:RU365090}.
FT DOMAIN 175..316
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 638 AA; 70303 MW; 45EB81BE16DB4FCA CRC64;
MVAKYKEHIS LKEVASILKE NLTPLSKRVR LSTTDTNSSL VGKVLMEDVY AERNIPHYPA
SAVDGYAICS SDTSYANPAS PVEIPEGKFL WVNTGAFVPE RFDAVVMVED TSVEGDSLYV
FNAVSKGANI RPIGEDVSKG RIIGRKGELL TPFHKALFAA AGVEEVEVRA PIKTCFIPTG
NEIVDIRETN TKQLAPGKVP ETNSLLLSEL FQTWGFHLDV LPLIPDDPEL LKGSIKQAVE
EYDLVLVGAG TAKGKRDYSA EVLAEQGKML FRWLRMKPGR PVMMAVVKDK PVIALPGFPV
STLVASWTVV FPTLQILKRG DISESYLSEA VKTAKQVKTE LAEHYSTRQG ISEWLRVQCG
EVNGKTYSWV TSSGASSMMP LTEADGFSLV GEEVLELPKG SSIEVWVVKE NDWINRAVYQ
GSNDPGIEHL VGYVRDRGGD LIIRSVGSLG GVTALARGEC HMAACHLLDP KTGEYNTSYI
KRFDINDEWD RILLYRRLQG LIVKKGNPKR IVDVADLTRE DVVVVNRQPG SGTRVLLDYL
LSQTEIDPKQ IRGYDNIAVT HFDAASKVAY GNADVVVGIK AVADALDLDF IPLVEEPFEV
IIPRAFLDHP GVKAFRDAIT DKVWKETIIK LGGYKLEQ
//
