(data stored in SCRATCH zone)

SWISSPROT: D6ZBR2_SEGRD

ID   D6ZBR2_SEGRD            Unreviewed;       423 AA.
AC   D6ZBR2;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 43.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   OrderedLocusNames=Srot_0402 {ECO:0000313|EMBL:ADG96889.1};
OS   Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 /
OS   DSM 44985 / JCM 13578).
OC   Bacteria; Actinobacteria; Corynebacteriales; Segniliparaceae;
OC   Segniliparus.
OX   NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG96889.1, ECO:0000313|Proteomes:UP000002247};
RN   [1] {ECO:0000313|EMBL:ADG96889.1, ECO:0000313|Proteomes:UP000002247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC   {ECO:0000313|Proteomes:UP000002247};
RX   PubMed=21304703; DOI=10.4056/sigs.791633;
RA   Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M.,
RA   Schneider S., Bruce D., Goodwin L., Pitluck S., Liolios K.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chertkov O., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P.;
RT   "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT   1076).";
RL   Stand. Genomic Sci. 2:203-211(2010).
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; CP001958; ADG96889.1; -; Genomic_DNA.
DR   RefSeq; WP_013137345.1; NC_014168.1.
DR   STRING; 640132.Srot_0402; -.
DR   EnsemblBacteria; ADG96889; ADG96889; Srot_0402.
DR   KEGG; srt:Srot_0402; -.
DR   eggNOG; ENOG4105CVM; Bacteria.
DR   eggNOG; COG0303; LUCA.
DR   HOGENOM; HOG000280651; -.
DR   KO; K03750; -.
DR   OMA; MTGAMVP; -.
DR   OrthoDB; 651103at2; -.
DR   BioCyc; SROT640132:G1GLH-405-MONOMER; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000002247; 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   GO; GO:0032324; P:molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00887; MoeA; 1.
DR   Gene3D; 2.40.340.10; -; 1.
DR   Gene3D; 3.40.980.10; -; 1.
DR   InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR   InterPro; IPR001453; MoaB/Mog_dom.
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   PANTHER; PTHR10192; PTHR10192; 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; SSF53218; SSF53218; 1.
DR   SUPFAM; SSF63867; SSF63867; 1.
DR   SUPFAM; SSF63882; SSF63882; 1.
DR   TIGRFAMs; TIGR00177; molyb_syn; 1.
PE   3: Inferred from homology;
DR   PRODOM; D6ZBR2.
DR   SWISS-2DPAGE; D6ZBR2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002247};
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:UP000002247};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN      179    339       MoCF_biosynth. {ECO:0000259|SMART:
FT                                SM00852}.
SQ   SEQUENCE   423 AA;  44255 MW;  4064A24D1F9CA96F CRC64;
     MRSVEEHQRR VAELIRAPKP VRLPLGQALG RVLAEDITAQ IPLPSFDNSA MDGYAARAED
     LAGASEQHPV VLPVAADIPA GSPATFALAP QSVHRIMTGA CLPPGADAIL PFESTDRGAE
     FVRAHAPAKP GAHIRRAGED LRRGERALAA GARLRAPQIG LIAALGFAEV AVFAPLQVLV
     LSTGSELTAP GQPLERGRIY ESNSPMLAAA VEETGAVAHR LRFVPDSVAA FHARIGQALA
     ELGEVDLILT SGGVSAGEYE VVKQAFAEGQ TEFGQVEFVS VAMQPGKPQG CGVYSPARRA
     HAESAPPTAG AATALVALPG NPVSAQVSFE VFLREPLAAA MGHPRPRRQV LRLPLAEPVP
     RSPAGKRQFL RGVLAQDRSS VSPFGPPGSH FLRSMALSDC LVDIPAGTTS LPEGAEVDVW
     DLG
//

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