GenomeNet

Database: UniProt
Entry: U5W0Z7_9ACTN
LinkDB: U5W0Z7_9ACTN
Original site: U5W0Z7_9ACTN 
ID   U5W0Z7_9ACTN            Unreviewed;       387 AA.
AC   U5W0Z7;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   ORFNames=AFR_22745 {ECO:0000313|EMBL:AGZ42819.1};
OS   Actinoplanes friuliensis DSM 7358.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=1246995 {ECO:0000313|EMBL:AGZ42819.1, ECO:0000313|Proteomes:UP000017746};
RN   [1] {ECO:0000313|EMBL:AGZ42819.1, ECO:0000313|Proteomes:UP000017746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7358 {ECO:0000313|EMBL:AGZ42819.1,
RC   ECO:0000313|Proteomes:UP000017746};
RX   PubMed=24637369; DOI=10.1016/j.jbiotec.2014.03.011;
RA   Ruckert C., Szczepanowski R., Albersmeier A., Goesmann A., Fischer N.,
RA   Steinkamper A., Puhler A., Biener R., Schwartz D., Kalinowski J.;
RT   "Complete genome sequence of the actinobacterium Actinoplanes friuliensis
RT   HAG 010964, producer of the lipopeptide antibiotic friulimycin.";
RL   J. Biotechnol. 178:41-42(2014).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP006272; AGZ42819.1; -; Genomic_DNA.
DR   RefSeq; WP_023363308.1; NC_022657.1.
DR   AlphaFoldDB; U5W0Z7; -.
DR   STRING; 1246995.AFR_22745; -.
DR   KEGG; afs:AFR_22745; -.
DR   PATRIC; fig|1246995.3.peg.4610; -.
DR   eggNOG; COG0303; Bacteria.
DR   HOGENOM; CLU_010186_1_2_11; -.
DR   OrthoDB; 3196725at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000017746; 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; 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; 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:UP000017746};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          171..307
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   387 AA;  38526 MW;  7B5B61B4AE46CEA2 CRC64;
     MPSIDHSPVP WRTAVKIATG AATPLPPSVV PSSEATGRVL AAPVLARGDL PGFDASAMDG
     YAVAGRGPWR VLGQVYAGGP VWPAPLGAGE AVEIMTGAVV PAGTVAVLPY ETADLNAAGP
     GPKAHIRRAG EDARAGDELL PAGRLVTPAV AGLLAQAGAD SVTVHGRPTV RLVVTGDELV
     TAGVPGPGQV RDVFTPMVSA LVAAAGGVVT DAVLIGDEPE LLAAALTTAD ADVVVVTGSS
     SAGAADHLHG VLNGIGARRL VDQVACRPGR PQLLAELPGT RWVVGLPGNP FAGLVACVTV
     LGPLLHGLSG RAAPDLIRLP VTGDLRPAPG VTRLVPVRLA GDHALVVPGG RPASLRGAAL
     ADALAVLEDG WTTGIPADLI PLNGLNS
//
DBGET integrated database retrieval system