ID F9TA09_9VIBR Unreviewed; 411 AA.
AC F9TA09;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN ORFNames=IX91_19140 {ECO:0000313|EMBL:AIW16216.1};
OS Vibrio tubiashii ATCC 19109.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio; Vibrio oreintalis group.
OX NCBI_TaxID=1051646 {ECO:0000313|EMBL:AIW16216.1, ECO:0000313|Proteomes:UP000030071};
RN [1] {ECO:0000313|EMBL:AIW16216.1, ECO:0000313|Proteomes:UP000030071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19109 {ECO:0000313|EMBL:AIW16216.1,
RC ECO:0000313|Proteomes:UP000030071};
RA Richards G.P., Needleman D.S., Watson M.A., Bono J.L.;
RT "First Complete Genome Sequence of the Shellfish Pathogen Vibrio
RT tubiashii.";
RL Submitted (AUG-2014) 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; CP009355; AIW16216.1; -; Genomic_DNA.
DR RefSeq; WP_004746845.1; NZ_CP009355.1.
DR AlphaFoldDB; F9TA09; -.
DR STRING; 1051646.IX91_19140; -.
DR KEGG; vtu:IX91_19140; -.
DR PATRIC; fig|1051646.9.peg.3746; -.
DR eggNOG; COG0303; Bacteria.
DR HOGENOM; CLU_010186_7_0_6; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000030071; Chromosome 2.
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; IPR008284; MoCF_biosynth_CS.
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.
DR PROSITE; PS01079; MOCF_BIOSYNTHESIS_2; 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}.
FT DOMAIN 184..321
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 411 AA; 44448 MW; 8B26335EA51C415C CRC64;
MGCCDAPGLM PIEEAMDKML SPIKPIQTTL QLPLAEAIGF VLAEDILSPI FVPPFDNSAM
DGYALRLADL AQNNVMPLAG KSFAGQPFDG EWPQGTCIRI MTGAKIPDGC DAVIMQENTE
VLEQGIQFNQ SDVKPQNNIR PMGDDIKQGD VVLNKGARLT SRDIPMIATL GISHVTVVRK
PRVAFFSTGD ELKPLGEPLA EGQIYDSNRY GIKPLIENFG CEAIDLGIIP DCPETLKATF
EKAQSLADVV VTSGGVSVGE ADYTKDILEK LGQIGFWKLA IKPGKPFAFG KLSTAWFCGL
PGNPVSAVLT MYVLVQPLLA KLAGHTEWAA PESIPATTRS AFKKAPGRTD YQRGIYSIED
GKFVVETTGN QSSGAFRSMS LANCFVVLER ERGRVEVGET VNIQLFNPTL Y
//