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Database: UniProt
Entry: J3D5Z1_9BURK
LinkDB: J3D5Z1_9BURK
Original site: J3D5Z1_9BURK 
ID   J3D5Z1_9BURK            Unreviewed;       426 AA.
AC   J3D5Z1;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   ORFNames=PMI16_03565 {ECO:0000313|EMBL:EJL85261.1};
OS   Herbaspirillum sp. CF444.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herbaspirillum.
OX   NCBI_TaxID=1144319 {ECO:0000313|EMBL:EJL85261.1, ECO:0000313|Proteomes:UP000007296};
RN   [1] {ECO:0000313|EMBL:EJL85261.1, ECO:0000313|Proteomes:UP000007296}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF444 {ECO:0000313|EMBL:EJL85261.1,
RC   ECO:0000313|Proteomes:UP000007296};
RX   PubMed=23045501; DOI=10.1128/JB.01243-12;
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA   Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT   "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT   sequences from diverse bacteria isolated from the rhizosphere and
RT   endosphere of Populus deltoides.";
RL   J. Bacteriol. 194:5991-5993(2012).
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:EJL85261.1}.
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DR   EMBL; AKJW01000077; EJL85261.1; -; Genomic_DNA.
DR   AlphaFoldDB; J3D5Z1; -.
DR   STRING; 1144319.PMI16_03565; -.
DR   PATRIC; fig|1144319.3.peg.3618; -.
DR   eggNOG; COG0303; Bacteria.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000007296; 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; 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; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 1.
DR   PANTHER; PTHR10192:SF34; MOLYBDOPTERIN MOLYBDENUMTRANSFERASE; 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          197..341
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   426 AA;  45977 MW;  E32DE020C513AE08 CRC64;
     MEAFPRQPIF LSMLVKPPLL SVAEATRFLL KAVVPLTDTE IVPTLEANGR VLAAAQVSQI
     NVPGMDNSQM DGYAVRAAEC AGGETRLRVS QRIPAGHVGT RLEPGTAARI FTGAMVPEGA
     DAIVMQEACE LVNDADGDHV IVRHAPEAGE WIRRIGEDIK SASTILPAGL RLRPQELGLA
     ASVGLATLPV VRKLRVAVFF TGDELTMPGE ALKPGAIYNS NRFLLRGLLE NLGCEVQDFG
     IVPDQLQATR DTLRAAAASH DLIITSGGVS VGEEDHVKPA VEAEGRLNMW QIAMKPGKPL
     AFGEIHRRGG TAEKAFFIGL PGNPVSTFVT FLIFVRPFLL RLQGVEHVAP RALTMRADFN
     WPKADRRQEF LRARCNDRGG LDLFPHQGSG VLTSTVWGDG LIDNAPGKTI AEGDPVRFIP
     FDNLLN
//
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