ID A0A1H3QUN4_9CLOT Unreviewed; 411 AA.
AC A0A1H3QUN4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|ARBA:ARBA00021108, ECO:0000256|RuleBase:RU365090};
DE EC=2.10.1.1 {ECO:0000256|ARBA:ARBA00013269, ECO:0000256|RuleBase:RU365090};
GN ORFNames=SAMN05192546_11097 {ECO:0000313|EMBL:SDZ16429.1};
OS Tindallia californiensis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Tindallia.
OX NCBI_TaxID=159292 {ECO:0000313|EMBL:SDZ16429.1, ECO:0000313|Proteomes:UP000199230};
RN [1] {ECO:0000313|EMBL:SDZ16429.1, ECO:0000313|Proteomes:UP000199230}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APO {ECO:0000313|EMBL:SDZ16429.1,
RC ECO:0000313|Proteomes:UP000199230};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNPV01000010; SDZ16429.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3QUN4; -.
DR STRING; 159292.SAMN05192546_11097; -.
DR OrthoDB; 9804758at2; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000199230; Unassembled WGS sequence.
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:UP000199230};
KW Transferase {ECO:0000256|RuleBase:RU365090, ECO:0000313|EMBL:SDZ16429.1}.
FT DOMAIN 182..320
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 411 AA; 44482 MW; C5671A2EDF467763 CRC64;
MRTNVTLEEA LALLLDECPQ TQSIHVPILD SLGGVLAEDI VSDINIPPFD RSPLDGYALR
SVDSQGASPD QPIELDVIDY VPAGSVSEKC VKDYQAVRIM TGAKIPLGAD VVIRQEEVEN
VGEKILIKAP MSTMENISRV GEDIHVNQMV IKAGTVIEPA EIGLMATLGK SYVSVYMKPR
VAILSTGDEL LEIQQPLQDG KIRNSNSYTI AAQVKKTGGK ALMLGVCGDD IESISEKLRA
GLGIADIVIT TGGVSVGDKD LVKESFMNAG AEMLFWKVRM KPGTPIAVAR LGKKLLIGLS
GNPAAAFITF EQFVRPLVLK MMGREKHRLM NVETILENDF SKVSNQNRFV RGTTVYRDGS
FYTKFPGKHS SGVLSSLSGN NSLFYVPAGT GPYEKGQKVS IQLLDQPEVK S
//
