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Database: UniProt
Entry: F9T263_9VIBR
LinkDB: F9T263_9VIBR
Original site: F9T263_9VIBR 
ID   F9T263_9VIBR            Unreviewed;       589 AA.
AC   F9T263;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   ORFNames=IX91_07925 {ECO:0000313|EMBL:AIW14125.1};
OS   Vibrio tubiashii ATCC 19109.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio; Vibrio oreintalis group.
OX   NCBI_TaxID=1051646 {ECO:0000313|EMBL:AIW14125.1, ECO:0000313|Proteomes:UP000030071};
RN   [1] {ECO:0000313|EMBL:AIW14125.1, ECO:0000313|Proteomes:UP000030071}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19109 {ECO:0000313|EMBL:AIW14125.1,
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; CP009354; AIW14125.1; -; Genomic_DNA.
DR   RefSeq; WP_004743528.1; NZ_CP009354.1.
DR   AlphaFoldDB; F9T263; -.
DR   STRING; 1051646.IX91_07925; -.
DR   KEGG; vtu:IX91_07925; -.
DR   PATRIC; fig|1051646.9.peg.1572; -.
DR   eggNOG; COG0303; Bacteria.
DR   eggNOG; COG1763; Bacteria.
DR   HOGENOM; CLU_010186_5_0_6; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000030071; Chromosome 1.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
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; cd03116; MobB; 1.
DR   CDD; cd00887; MoeA; 1.
DR   Gene3D; 2.20.25.120; -; 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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR   InterPro; IPR001453; MoaB/Mog_dom.
DR   InterPro; IPR004435; MobB_dom.
DR   InterPro; IPR012182; MobB_MoeA.
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   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00176; mobB; 1.
DR   NCBIfam; TIGR00177; molyb_syn; 1.
DR   PANTHER; PTHR10192:SF5; GEPHYRIN; 1.
DR   PANTHER; PTHR10192; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 1.
DR   Pfam; PF03205; MobB; 1.
DR   Pfam; PF00994; MoCF_biosynth; 1.
DR   Pfam; PF03454; MoeA_C; 1.
DR   Pfam; PF03453; MoeA_N; 1.
DR   PIRSF; PIRSF036618; MobB_MoeA; 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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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          363..500
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   589 AA;  64234 MW;  2F71290D18D38F7E CRC64;
     MTLNLPIPIL GFAAYSGTGK TTLLEALLPK LTEAGLRIGM LKHAHHNFDV DKEGKDSYRL
     RKAGASQMLI SSRNRFALMT ETPEQESEFA YLLSRFDTDK LDVILVEGCK NIAFPKIELH
     RAAVGKPWLY NNDDNIIAIA ADSIVEDSDL PQMSINDLDA IARFVTEYVR SQAEPKKNEA
     ACCDTLSPAF LSVEQGREKI LSLVNPVPES ELCPITQASG RVLFEDIISP VNVPQYTNSA
     MDGFAIRGED ADLDSFEVVA EVFAGHAYDH SLEKGQAVKI MTGAPTPEGG DTVIMREQAQ
     HNGDIVTFSA SIKVGQNVRQ AGEDLAIGSS VFTTGQRIAS PEMGMIASLG MAECSVYRKL
     KVAIFSTGDE VQDPGSEQKQ NSIYDSNRFT IMGMLETLGC EILDFGIIED DEALMIEALE
     NAASQADVVM TSGGVSVGDA DYIKLALEKL GQIDFWRINM RPGRPLAFGQ IQNKPFFGLP
     GNPVAVMVSF INFVEPALRK MQGEQGWQPL KVNAIATESL RSRQGRTEFS RGIYELDHRG
     QLTVRTTGKQ GSGILRSMSE ANCLIEISPA IDTVKVGESV TIIPLQGRI
//
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