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Database: UniProt
Entry: K9SDH4_9CYAN
LinkDB: K9SDH4_9CYAN
Original site: K9SDH4_9CYAN 
ID   K9SDH4_9CYAN            Unreviewed;       414 AA.
AC   K9SDH4;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   ORFNames=GEI7407_3559 {ECO:0000313|EMBL:AFY68026.1};
OS   Geitlerinema sp. PCC 7407.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Geitlerinematales;
OC   Geitlerinemataceae; Geitlerinema.
OX   NCBI_TaxID=1173025 {ECO:0000313|EMBL:AFY68026.1, ECO:0000313|Proteomes:UP000010383};
RN   [1] {ECO:0000313|EMBL:AFY68026.1, ECO:0000313|Proteomes:UP000010383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7407 {ECO:0000313|EMBL:AFY68026.1,
RC   ECO:0000313|Proteomes:UP000010383};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA   Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA   Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA   Pitluck S., Woyke T., Kerfeld C.;
RT   "Finished genome of Geitlerinema sp. PCC 7407.";
RL   Submitted (MAY-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; CP003591; AFY68026.1; -; Genomic_DNA.
DR   RefSeq; WP_015173590.1; NC_019703.1.
DR   AlphaFoldDB; K9SDH4; -.
DR   STRING; 1173025.GEI7407_3559; -.
DR   KEGG; gei:GEI7407_3559; -.
DR   PATRIC; fig|1173025.3.peg.3973; -.
DR   eggNOG; COG0303; Bacteria.
DR   HOGENOM; CLU_010186_7_1_3; -.
DR   OrthoDB; 9804758at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000010383; 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   Reference proteome {ECO:0000313|Proteomes:UP000010383};
KW   Transferase {ECO:0000256|RuleBase:RU365090, ECO:0000313|EMBL:AFY68026.1}.
FT   DOMAIN          179..322
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   414 AA;  43334 MW;  6B6835B380CD49FE CRC64;
     MLSVYEAETR IQAQIQPFSA ENDQERVPLL QAAGRVLAMP VQSGLDFPHW DNASMDGYAV
     RHEDLATVPV TLTIGEEIPA GYQPQQVVAA GQAARILTGS MMPAGADTVV MQENTERSGD
     RVTILRAPEP QANVRHRGAF ARAGAPLLAA GLVLNGPEIA VLAAAQCVQV PVFRRPRVAI
     LSTGSELVSP EQPLAPGQIV DSNQYALAAL VAQSGGEALP LGIVPDQPEA LRAAMAGAIA
     QADVVISSGG VSVGDYDYID GLLAELGGTI HVQSVAIKPG KPLTVATFGR SGQRPVLYFG
     LPGNPVSSLM SFWRFVQPAI RRLGGQARGW EPVFVTGRSR QDLRGGGQRE TYLWGRLTLV
     GGAYEFELAG GGHSSGNLIN LAATNALAVV PVGQTLVPAG EPTRILQVGA VFPG
//
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