ID A0A0N9VET1_9GAMM Unreviewed; 401 AA.
AC A0A0N9VET1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN ORFNames=AOY20_09405 {ECO:0000313|EMBL:ALH95728.1};
OS Acinetobacter equi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1324350 {ECO:0000313|EMBL:ALH95728.1, ECO:0000313|Proteomes:UP000064939};
RN [1] {ECO:0000313|EMBL:ALH95728.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=114 {ECO:0000313|EMBL:ALH95728.1};
RX PubMed=26620413;
RA Poppel M.T., Skiebe E., Laue M., Bergmann H., Ebersberger I., Garn T.,
RA Fruth A., Baumgardt S., Busse H.J., Wilharm G.;
RT "Acinetobacter equi sp. nov. isolated from horse faeces.";
RL Int. J. Syst. Evol. Microbiol. 0:0-0(2015).
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; CP012808; ALH95728.1; -; Genomic_DNA.
DR RefSeq; WP_054581619.1; NZ_CP012808.1.
DR AlphaFoldDB; A0A0N9VET1; -.
DR STRING; 1324350.AOY20_09405; -.
DR KEGG; aei:AOY20_09405; -.
DR OrthoDB; 9804758at2; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000064939; 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:UP000064939};
KW Transferase {ECO:0000256|RuleBase:RU365090}.
FT DOMAIN 175..313
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 401 AA; 44281 MW; 441E9D1DA6EDBE0E CRC64;
MSLIPYAQAF DKLIQQLNAQ NKTELVAIEE VQGRVLAASI EAQFDSPIFD NSAMDGYAIC
GIEQESWTLI DYVAAGDSTQ HIHLKSGQAV RIFTGSAVPL GTDAVIPQEN ISIQNHIIMS
LEPIKEKQHI RFKAEEFTEN DILVGKNQII TATHIGVFAS QGLTEVLCYA PLKVTVFSSG
NELQSLGKEL LENQIYDSNR LMLLSLLKNY SFIQYFDGGV LPDDELIIEE QLSRAEKQSD
VILISGGASV GDKDYTKQVL EKIGEVQHWK LAIKPGKPFA WGKINNTKVF VLPGNPVACW
VTYLILVLPA LKVLSGIQPN LVLPKKIQAK AQFNTHKAQS RLQFLRGNIA IVEGQVQAFI
HALQSSAMLA NCANSNALVM IPENETVQHG QMIELIYLDE I
//
