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-MAY-2013, entry version 86.
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 (By similarity).
CC -!- CATALYTIC ACTIVITY: Adenylyl-molybdopterin + molybdate =
CC molybdenum cofactor + AMP.
CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC -!- SIMILARITY: Belongs to the MoeA family.
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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 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; KLAMQPG; -.
DR ProtClustDB; CLSK896330; -.
DR UniPathway; UPA00344; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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; MoCF_biosynth; 1.
DR SUPFAM; SSF63867; MoeA_C; 1.
DR SUPFAM; SSF63882; MoeA_N; 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; 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
//
