(data stored in ACNUC7421 zone)

SWISSPROT: A0LE83_SYNFM

ID   A0LE83_SYNFM            Unreviewed;       544 AA.
AC   A0LE83;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 64.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   OrderedLocusNames=Sfum_0032 {ECO:0000313|EMBL:ABK15735.1};
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK15735.1, ECO:0000313|Proteomes:UP000001784};
RN   [1] {ECO:0000313|EMBL:ABK15735.1, ECO:0000313|Proteomes:UP000001784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10017 / MPOB {ECO:0000313|Proteomes:UP000001784};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J.,
RA   Sieber J., Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL   Submitted (OCT-2006) 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|RuleBase:RU365090}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O +
CC         Mo-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;
CC         Evidence={ECO:0000256|RuleBase:RU365090};
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|RuleBase:RU365090}.
CC   -!- SIMILARITY: Belongs to the MoeA family.
CC       {ECO:0000256|RuleBase:RU365090}.
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DR   EMBL; CP000478; ABK15735.1; -; Genomic_DNA.
DR   RefSeq; WP_011696908.1; NC_008554.1.
DR   STRING; 335543.Sfum_0032; -.
DR   EnsemblBacteria; ABK15735; ABK15735; Sfum_0032.
DR   KEGG; sfu:Sfum_0032; -.
DR   eggNOG; ENOG4105C43; Bacteria.
DR   eggNOG; COG0303; LUCA.
DR   eggNOG; COG2191; LUCA.
DR   HOGENOM; HOG000009979; -.
DR   OMA; CQGEAPY; -.
DR   OrthoDB; 651103at2; -.
DR   BioCyc; SFUM335543:G1G7I-34-MONOMER; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000001784; Chromosome.
DR   Gene3D; 3.40.980.10; -; 1.
DR   InterPro; IPR003814; FwdEsu_dom.
DR   InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR   InterPro; IPR001453; MoaB/Mog_dom.
DR   InterPro; IPR038987; MoeA-like.
DR   PANTHER; PTHR10192; PTHR10192; 1.
DR   Pfam; PF02663; FmdE; 1.
DR   Pfam; PF00994; MoCF_biosynth; 1.
DR   SMART; SM00852; MoCF_biosynth; 1.
DR   SUPFAM; SSF53218; SSF53218; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0LE83.
DR   SWISS-2DPAGE; A0LE83.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001784};
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|RuleBase:RU365090};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001784};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN      379    511       MoCF_biosynth. {ECO:0000259|SMART:
FT                                SM00852}.
SQ   SEQUENCE   544 AA;  58896 MW;  8EDB953A88151251 CRC64;
     MKIGRYSYDE YLELVKSFHG YAAPGLMMGG VMVDLALSRM PEGVLFDAVC ETASCLPDAV
     QLLTPCTVGN GWVRVLNLGR YALSLYDKST GSGVRVFVDA AKIRAWPEAE AWLFKLKPKA
     AQDTGLLLRQ IKEAGYGIYG VQDIRIQPQF LVRHHKGSIG TCTLCGEPYP ADDGGICRGC
     QGEAPYAVPG EVESDGFPDG PDLLAVPVQD AVGRSMLHDM TQILPGKSKG AAFRRGQQIS
     VGDLCRLQQM GRQRVYVDQG NTPDGEWIHE DQAALAFARA MAGEGVRFVE PPREGKINFV
     ADRDGLFLVE EESLEEFNMV AGVMCASRRG YTLVRNGRML GGTRAIPLYL PRSAFMKALA
     VLRYGPLFRV LPMRKARVGI LVTGSEVFQG LIEDRFIPII GAKVEALDCK VVKAVIVPDD
     RVAIRDGVHE LVRAGADLLV TTAGLSVDPD DVTRQGLKDA GAMDMLYGAP VLPGAMTLLA
     RIGSVQVMGV PACALYFKTT SFDLLFPRLL AGVDIARRDL AKLGHGSFCL ECKACTFPKC
     PFGG
//

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