GenomeNet

Database: UniProt
Entry: A2SIT9_METPP
LinkDB: A2SIT9_METPP
Original site: A2SIT9_METPP 
ID   A2SIT9_METPP            Unreviewed;       433 AA.
AC   A2SIT9;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   24-JAN-2024, entry version 90.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   OrderedLocusNames=Mpe_A2523 {ECO:0000313|EMBL:ABM95478.1};
OS   Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Methylibium.
OX   NCBI_TaxID=420662 {ECO:0000313|EMBL:ABM95478.1, ECO:0000313|Proteomes:UP000000366};
RN   [1] {ECO:0000313|EMBL:ABM95478.1, ECO:0000313|Proteomes:UP000000366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1232 / LMG 22953 / PM1
RC   {ECO:0000313|Proteomes:UP000000366};
RX   PubMed=17158667; DOI=10.1128/JB.01259-06;
RA   Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA   Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA   Hristova K.R.;
RT   "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT   proteobacterium Methylibium petroleiphilum PM1.";
RL   J. Bacteriol. 189:1931-1945(2007).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000555; ABM95478.1; -; Genomic_DNA.
DR   RefSeq; WP_011830111.1; NC_008825.1.
DR   AlphaFoldDB; A2SIT9; -.
DR   STRING; 420662.Mpe_A2523; -.
DR   KEGG; mpt:Mpe_A2523; -.
DR   eggNOG; COG0303; Bacteria.
DR   HOGENOM; CLU_010186_7_0_4; -.
DR   OMA; VDHVHPT; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000000366; 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; 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.
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:UP000000366};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          203..344
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   433 AA;  45575 MW;  EE3BEEAD30053317 CRC64;
     MDSPTPSALP SIEQIASCIA GYDPNALAVA QAQDFIARFV PKVGAVEQLA LRSALGRVLA
     HDIISPIDVP AHDNSAMDGY ALRGADLRDG QPTTLRLAGT GFAGQQFEGR VAAGECVRIM
     TGAVMPAGLD TVVPQEFTSV ADGAVTLPAG VVRTGDNRRL AGEDLARGEA ALQAGRVLRP
     ADIGMLASLG RAEVPVRRRL RVAFFSTGDE LRSIGEPLEA GCVYDSNRYT IHGMLTRLGV
     ELLDLGVVRD DPAALEAAFR SACENADAVI TSGGVSVGEA DHTKQVMARL GEVAFWRIAM
     RPGRPMAFGR VASNGRTAVL FGLPGNPVAV MVTFYAFVRD ALLAMAGATP QSLPLLRART
     AEAIRKKPGR TEYQRGIVSR AADGDWDVQL TGAQGSGILR SMSVANGLVV LHHEQASVER
     GGYVDVLPFD GLV
//
DBGET integrated database retrieval system