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Database: UniProt
Entry: X0QSU5_9GAMM
LinkDB: X0QSU5_9GAMM
Original site: X0QSU5_9GAMM 
ID   X0QSU5_9GAMM            Unreviewed;       371 AA.
AC   X0QSU5;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   ORFNames=JCM18900_12525 {ECO:0000313|EMBL:GAF53916.1};
OS   Psychrobacter sp. JCM 18900.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Psychrobacter.
OX   NCBI_TaxID=1298608 {ECO:0000313|EMBL:GAF53916.1, ECO:0000313|Proteomes:UP000019500};
RN   [1] {ECO:0000313|EMBL:GAF53916.1, ECO:0000313|Proteomes:UP000019500}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 18900 {ECO:0000313|EMBL:GAF53916.1,
RC   ECO:0000313|Proteomes:UP000019500};
RA   Kudo T., Kidera A., Kida M., Kawauchi A., Shimizu R., Nakahara T.,
RA   Zhang X., Yamada A., Amano M., Hamada Y., Taniyama S., Arakawa O.,
RA   Yoshida A., Oshima K., Suda W., Kuwahara H., Nogi Y., Kitamura K., Yuki M.,
RA   Iida T., Moriya S., Inoue T., Hongo Y., Hattori M., Ohkuma M.;
RT   "Draft Genome Sequences of Psychrobacter Strains JCM 18900, JCM 18901, JCM
RT   18902, and JCM 18903, Isolated Preferentially from Frozen Aquatic
RT   Organisms.";
RL   Genome Announc. 2:e00280-14(2014).
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:GAF53916.1}.
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DR   EMBL; BAWG01000010; GAF53916.1; -; Genomic_DNA.
DR   AlphaFoldDB; X0QSU5; -.
DR   eggNOG; COG0303; Bacteria.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000019500; 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: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          135..278
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   371 AA;  40072 MW;  FEF8BB1DBDCD97AC CRC64;
     MDGYAIAKGS ELSENSNIEI VGESQAGSAY TGKTTAGQGV RIFTGAVVPD CCDTVIMQEN
     TNFADIKATV DKSQPYNITL TQTAKVGNNI RSQGEEIESG EAVLKIGKRL NPADISLLAN
     LGISQVNVFQ PLVVGVLATG DELVAIGNEL QSLAQIYNSN TPTLKSLLSD LPITIRDYGI
     IPDNLEQTTI AVNEAMQDCD VLISTAGVSV GDYDFLTTVI ETLGQINHYK VAMKPGKPFV
     FGELNKNLDK PVLYFGLPGN PLSTVVGALQ FVIPALWQMS GASVSEQPMP LTIKAKLISD
     IRKSPGRKDF QRGVLSRDDT GHYQVECFSR QQSHRIKQLS RANCFIVLDK DSGNVAAGKD
     VVVQPFPWLH R
//
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