ID   Q87PK6_VIBPA            Unreviewed;       592 AA.
AC   Q87PK6;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 105.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   OrderedLocusNames=VP1496 {ECO:0000313|EMBL:BAC59759.1};
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926 {ECO:0000313|EMBL:BAC59759.1, ECO:0000313|Proteomes:UP000002493};
RN   [1] {ECO:0000313|EMBL:BAC59759.1, ECO:0000313|Proteomes:UP000002493}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633 {ECO:0000313|Proteomes:UP000002493};
RX   PubMed=12620739; DOI=10.1016/S0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
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; BA000031; BAC59759.1; -; Genomic_DNA.
DR   RefSeq; NP_797875.1; NC_004603.1.
DR   RefSeq; WP_005479452.1; NC_004603.1.
DR   AlphaFoldDB; Q87PK6; -.
DR   GeneID; 1189003; -.
DR   KEGG; vpa:VP1496; -.
DR   PATRIC; fig|223926.6.peg.1429; -.
DR   eggNOG; COG0303; Bacteria.
DR   eggNOG; COG1763; Bacteria.
DR   HOGENOM; CLU_010186_5_0_6; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000002493; 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   Reference proteome {ECO:0000313|Proteomes:UP000002493};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          366..503
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   592 AA;  64612 MW;  C6685C57ECAAD806 CRC64;
     MKHTLNIPIL GFAAYSGTGK TTLLEALLPK LTEAGLRIGM LKHAHHNFDV DKPGKDSYRL
     RKAGASQMLI ASRNRFALMT ETPEAEAEFE YLLTRFDEDK LDVVLVEGCK NIAFPKIELH
     REEVGKPWLY PHDENIIAIA SDSAELDSEL PQMNINDLDA IAQFVLQYVQ DAKAPKSKEK
     DAACCDTLSP AFLSVVQGQE KILSLVNTVS EIEACKIENA YGRVLAEDII SPVNVPQYTN
     SAMDGYAIRS DDVDRDSYQI VAEVMAGHAY DQPLEVGQAV KIMTGAPTPR NGDTVVMREQ
     ASQEGDKVTF NGAHIKAGQN VRQAGEDLAI GSDVFTAGTR LASPEMGMIA SLGFGEANVF
     RKLKVAVFST GDEVQAPGTE QKANSIYDSN RFTIMGMLEK LGCEILDFGI LEDNEQLMIE
     ALENASAQAD VVMTSGGVSV GDADYIKLAL DKLGQVDFWR INMRPGRPLA FGQINNKPFF
     GLPGNPVAVM VSFINFVEPA LRKMQGEQGW KPLKVKAIAT ENLRSRQGRT EFSRGIYELD
     DTGRLTVRTT GKQGSGILRS MSDANCLIEI SPAIDTVKAG ESVTIIPLQG RI
//