ID A0A0T6A4U1_9BACT Unreviewed; 646 AA.
AC A0A0T6A4U1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN ORFNames=XU15_C0007G0056 {ECO:0000313|EMBL:KRT69982.1};
OS candidate division NC10 bacterium CSP1-5.
OC Bacteria; candidate division NC10.
OX NCBI_TaxID=1640516 {ECO:0000313|EMBL:KRT69982.1, ECO:0000313|Proteomes:UP000051123};
RN [1] {ECO:0000313|EMBL:KRT69982.1, ECO:0000313|Proteomes:UP000051123}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSP1-5 {ECO:0000313|EMBL:KRT69982.1};
RA Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT "Critical biogeochemical functions in the subsurface are associated with
RT bacteria from new phyla and little studied lineages.";
RL Submitted (MAY-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRT69982.1}.
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DR EMBL; LDXR01000007; KRT69982.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T6A4U1; -.
DR STRING; 1640516.XU15_C0007G0056; -.
DR PATRIC; fig|1640516.3.peg.1206; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000051123; 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 InterPro; IPR024370; PBP_domain.
DR NCBIfam; TIGR00177; molyb_syn; 1.
DR PANTHER; PTHR10192; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 1.
DR PANTHER; PTHR10192:SF16; MOLYBDOPTERIN MOLYBDENUMTRANSFERASE; 1.
DR Pfam; PF00994; MoCF_biosynth; 1.
DR Pfam; PF03454; MoeA_C; 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 Transferase {ECO:0000256|RuleBase:RU365090, ECO:0000313|EMBL:KRT69982.1}.
FT DOMAIN 180..317
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 646 AA; 69649 MW; 38942F0C0125F139 CRC64;
MARRKVYLEP IPLDEALQKF FGALEARGLL RPLSGELVPV DAALGRVTAR PVWAALSNPH
YNAAAMDGIA VRAEDTRAAS ETAPVRLRAR EQFQWVDTGD PILPPLNAVV MLEHLYPVGE
EEIEIHAPVP PWHHVRAMGE DMVATELILP EGHTLTPPDL GAIAGCGLGA VEVRQRPRVA
VIPTGSELVP PGRAVKPGEI IEFNSLMLCG MVREWGGEAN RTGIVPDDFP AIRAAVEEAV
ATHDVVVINA GSSAGSEDFT AAIVGELGEL LVHGIAIRPG HPVVLGIVRG RPVIGIPGYP
VSAVITCDLL VKPILYRLEG RAVPERPTLT ATMTRKILSP LGEDEFLRVK LGRVGNKVVA
TPLSRGAGVI MSLVRADGIV RIPRFSEGVH AGATVTVELL RRPEEIEKTI VAIGSHDLTL
DLLASLLRRR HPDLHLSSTN VGSLAGLLAL KRAEAHMAGS HLLDEETGEY NLPYVARLLP
GEKVVVLTLV HRDQGLILPK GNPKDITTLL DLAREDVAFV NRQKGAGTRI LLEYRLKQLG
IDPMRITGYE REEYTHLAVA AAVKAGVADV GLGILGAARA LNLDFIPLLK ERYDLIIPEP
HYRDPLLRPL LDLITSEGFK QEVEALGGYD TSETGRVVNG PAAPCR
//
