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Database: UniProt
Entry: M4NGH5_9GAMM
LinkDB: M4NGH5_9GAMM
Original site: M4NGH5_9GAMM 
ID   M4NGH5_9GAMM            Unreviewed;       417 AA.
AC   M4NGH5;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-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=R2APBS1_2903 {ECO:0000313|EMBL:AGG89979.1};
OS   Rhodanobacter denitrificans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Rhodanobacter.
OX   NCBI_TaxID=666685 {ECO:0000313|EMBL:AGG89979.1, ECO:0000313|Proteomes:UP000011859};
RN   [1] {ECO:0000313|EMBL:AGG89979.1, ECO:0000313|Proteomes:UP000011859}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2APBS1 {ECO:0000313|EMBL:AGG89979.1,
RC   ECO:0000313|Proteomes:UP000011859};
RG   US DOE Joint Genome Institute;
RA   Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Tapia R.,
RA   Munk A.C.C., Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E.,
RA   Ivanova N., Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L.,
RA   Peters L., Pitluck S., Woyke T., Prakash O., Elkins J., Brown S.,
RA   Palumbo A., Hemme C., Zhou J., Watson D., Jardine P., Kostka J., Green S.;
RT   "Complete genome of Rhodanobacter sp. 2APBS1.";
RL   Submitted (APR-2012) 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; CP003470; AGG89979.1; -; Genomic_DNA.
DR   RefSeq; WP_015448439.1; NZ_CP088918.1.
DR   AlphaFoldDB; M4NGH5; -.
DR   STRING; 666685.R2APBS1_2903; -.
DR   KEGG; rhd:R2APBS1_2903; -.
DR   eggNOG; COG0303; Bacteria.
DR   HOGENOM; CLU_010186_7_0_6; -.
DR   OrthoDB; 9804758at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000011859; Chromosome.
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          181..322
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   417 AA;  44346 MW;  5808A8C4E44FBB0F CRC64;
     MIGYHDALML ILECTRRLPE RPCPVDQALG RVLARPVSSP AALPPFDNAA MDGFALHAGQ
     ARLPAGSEHA VMGAQAAGDA LAQADGGAWE IMTGARMPAG MDTVVPVEQV EIVEQAGDGR
     PRRIRLSIDV EAGRHVRRCG EDVPLDAEVI PAGELLQAQH LALLAALGIA EVPVVRRPRV
     AIICTGRELV DDPGQPLQSG QIRNSNGPFL AVRLVAAGAQ VVYRQTVGDD PAAFVRALGE
     ALHAGATVVL STGAVSMGRH DFVPEALRGL GARIHFHKLR IRPGKPLLFA SLPDGALFFG
     LPGNPVSSAV GLRFFVEPAL RGMLGLPPER PLRLPLRQRF EQRAPLRCFL KGKLALAADG
     RLQAVLLDGQ ESFRIRPLLD TGGWVVLAED AQVREPGSMV EVYALGHLQP LAIGSEA
//
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