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Database: UniProt
Entry: C7MP73_CRYCD
LinkDB: C7MP73_CRYCD
Original site: C7MP73_CRYCD 
ID   C7MP73_CRYCD            Unreviewed;       467 AA.
AC   C7MP73;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   24-JAN-2024, entry version 67.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   OrderedLocusNames=Ccur_10220 {ECO:0000313|EMBL:ACU94713.1};
OS   Cryptobacterium curtum (strain ATCC 700683 / DSM 15641 / CCUG 43107 /
OS   12-3).
OC   Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC   Cryptobacterium.
OX   NCBI_TaxID=469378 {ECO:0000313|EMBL:ACU94713.1, ECO:0000313|Proteomes:UP000000954};
RN   [1] {ECO:0000313|EMBL:ACU94713.1, ECO:0000313|Proteomes:UP000000954}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700683 / DSM 15641 / 12-3
RC   {ECO:0000313|Proteomes:UP000000954};
RX   PubMed=21304644; DOI=10.40456/sigs.12260;
RA   Mavrommatis K., Pukall R., Rohde C., Chen F., Sims D., Brettin T.,
RA   Kuske C., Detter J.C., Han C., Lapidus A., Copeland A., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Ovchinnikova G., Pati A., Ivanova N., Chen A., Palaniappan K., Chain P.,
RA   D'haeseleer P., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Rohde M., Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Cryptobacterium curtum type strain (12-3).";
RL   Stand. Genomic Sci. 1:93-100(2009).
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|RuleBase:RU365090}.
CC   -!- SIMILARITY: Belongs to the MoeA family. {ECO:0000256|ARBA:ARBA00010763,
CC       ECO:0000256|RuleBase:RU365090}.
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DR   EMBL; CP001682; ACU94713.1; -; Genomic_DNA.
DR   RefSeq; WP_012803398.1; NC_013170.1.
DR   AlphaFoldDB; C7MP73; -.
DR   STRING; 469378.Ccur_10220; -.
DR   KEGG; ccu:Ccur_10220; -.
DR   eggNOG; COG0303; Bacteria.
DR   HOGENOM; CLU_010186_7_1_11; -.
DR   OMA; PVEDTHY; -.
DR   OrthoDB; 3196725at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000000954; 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   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; IPR036688; MoeA_C_domain_IV_sf.
DR   InterPro; IPR005110; MoeA_linker/N.
DR   InterPro; IPR036135; MoeA_linker/N_sf.
DR   PANTHER; PTHR10192:SF5; GEPHYRIN; 1.
DR   PANTHER; PTHR10192; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 1.
DR   Pfam; PF00994; MoCF_biosynth; 1.
DR   Pfam; PF03453; MoeA_N; 1.
DR   SMART; SM00852; MoCF_biosynth; 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:UP000000954};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          209..355
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
FT   REGION          378..404
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   467 AA;  50628 MW;  1A3CF10CB57B9E35 CRC64;
     MRDHSKHIQL SREDAVAQML AALDEVSEGF GWRGALAQTA SASDNQVTRH TRNVQRKLVE
     RVSLAESVDR VLAYDVVAQN DIPSALTCAM DSVALHWSDF ADLPEGQLPD TSKWVRGVNW
     QFANTGVAMP EGFDTAIVIE HVQVSTDEQH ITIDAAPSKP GAGTRPVGST MHRGDVLAQA
     GSLITPDLAA RIGTGNNASV DVIRRPRVAF IPTGNELIAP GVPFDPQHPD KFAAHGRTFE
     TNSVIVRAKC EQWGGQFIPF DIVLDRRDAI EDAIAHAVEV ADIVVLNAGS SKGSDDWSCE
     VMEEMGHMIY HQTNHGPGHH SSAAVIDGTP IIGISGPSGG ASFTLNFYLR PLMRAFMGLS
     PEAERIPVVL AEEFPAARSD RPKKHGNSVR GEERPMEHPE HEPGKPEFFA VKMLRIDHAE
     DGTLRAWPIA GRPGSAATLA ANAYYMLPTG TGIEAPKPGD IIWVEWR
//
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