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Database: UniProt
Entry: Q44243
LinkDB: Q44243
Original site: Q44243 
ID   MOEA_NOSS1              Reviewed;         436 AA.
AC   Q44243;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   01-OCT-2014, entry version 92.
DE   RecName: Full=Molybdopterin molybdenumtransferase;
DE            Short=MPT Mo-transferase;
DE            EC=2.10.1.1;
GN   Name=moeA; OrderedLocusNames=all5136;
OS   Nostoc sp. (strain PCC 7120 / UTEX 2576).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8682795;
RA   Ramaswamy K.S., Endley S., Golden J.W.;
RT   "Nitrate reductase activity and heterocyst suppression on nitrate in
RT   Anabaena sp. strain PCC 7120 require moeA.";
RL   J. Bacteriol. 178:3893-3898(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / UTEX 2576;
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S.,
RA   Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T.,
RA   Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
RA   Nakazaki N., Shimpo S., Sugimoto M., Takazawa M., Yamada M.,
RA   Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
CC   -!- FUNCTION: Catalyzes the insertion of molybdate into adenylated
CC       molybdopterin with the concomitant release of AMP. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: Adenylyl-molybdopterin + molybdate =
CC       molybdenum cofactor + AMP.
CC   -!- COFACTOR: Binds 1 magnesium ion per subunit. {ECO:0000250}.
CC   -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC   -!- SIMILARITY: Belongs to the MoeA family. {ECO:0000305}.
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DR   EMBL; U34309; AAC44505.1; -; Genomic_DNA.
DR   EMBL; BA000019; BAB76835.1; -; Genomic_DNA.
DR   PIR; AH2447; AH2447.
DR   RefSeq; NP_489176.1; NC_003272.1.
DR   RefSeq; WP_010999262.1; NC_003272.1.
DR   ProteinModelPortal; Q44243; -.
DR   STRING; 103690.all5136; -.
DR   EnsemblBacteria; BAB76835; BAB76835; BAB76835.
DR   GeneID; 1108740; -.
DR   KEGG; ana:all5136; -.
DR   PATRIC; 22780967; VBINosSp37423_5922.
DR   eggNOG; COG0303; -.
DR   HOGENOM; HOG000280651; -.
DR   KO; K03750; -.
DR   OMA; VGESYKK; -.
DR   OrthoDB; EOG66MQMC; -.
DR   UniPathway; UPA00344; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061599; F:molybdopterin molybdotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.340.10; -; 1.
DR   Gene3D; 3.40.980.10; -; 1.
DR   InterPro; IPR020817; Mo_cofactor_synthesis.
DR   InterPro; IPR008284; MoCF_biosynth_CS.
DR   InterPro; IPR005111; MoeA_C_domain_IV.
DR   InterPro; IPR005110; MoeA_linker/N.
DR   InterPro; IPR001453; Mopterin-bd_dom.
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; SSF53218; SSF53218; 1.
DR   SUPFAM; SSF63867; SSF63867; 1.
DR   SUPFAM; SSF63882; SSF63882; 1.
DR   TIGRFAMs; TIGR00177; molyb_syn; 1.
DR   PROSITE; PS01079; MOCF_BIOSYNTHESIS_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Magnesium; Metal-binding; Molybdenum;
KW   Molybdenum cofactor biosynthesis; Reference proteome; Transferase.
FT   CHAIN         1    436       Molybdopterin molybdenumtransferase.
FT                                /FTId=PRO_0000170988.
SQ   SEQUENCE   436 AA;  47332 MW;  65D73EA44536D561 CRC64;
     MQNKLSCEVK RNPHTPKPLH PYTPMPSVRD TANIIFNLVP KLDSQQDTEI VDLWAANGRI
     LATPVNSTLD FPHWDNSAMD GYAVRYEDVH NSNAEQPVSL EVVAEIPAGY QPKFTLQPGQ
     AARIFTGAVM PSGGDTVVMQ EKTRQENNRV FILTTPKPGE FVRLKAAYYQ AGTQLLPANT
     QLNAAEIAIL AASQCPQVKV YRRPRVAIFS TGDELVTLDQ PLQPGQIVDS NQYALAALVK
     QNGAEPILFG IVKDNPTALG ETISKAIANA DIVISSGGVS VGDYDYVDQI LASLGAKIHI
     RSVEMRPGKP LTVATFPTPP APIYLGLPGN PAAVLVTFWR FVQPVIRKLG GLAKGWEPVF
     VKVRSHDELH SDGKRETYIW GSLHLVDGLY EFHKAGGSHS SGNLINLAQT NALAVLPLGE
     TFISSGKDVL VLQLPI
//
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