GenomeNet

Database: UniProt
Entry: A0A0D3V8K0_9BACL
LinkDB: A0A0D3V8K0_9BACL
Original site: A0A0D3V8K0_9BACL 
ID   A0A0D3V8K0_9BACL        Unreviewed;       427 AA.
AC   A0A0D3V8K0;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|ARBA:ARBA00021108, ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|ARBA:ARBA00013269, ECO:0000256|RuleBase:RU365090};
GN   ORFNames=UB51_07660 {ECO:0000313|EMBL:AJS58395.1};
OS   Paenibacillus sp. IHBB 10380.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1566358 {ECO:0000313|EMBL:AJS58395.1, ECO:0000313|Proteomes:UP000032320};
RN   [1] {ECO:0000313|EMBL:AJS58395.1, ECO:0000313|Proteomes:UP000032320}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IHBB 10380 {ECO:0000313|EMBL:AJS58395.1,
RC   ECO:0000313|Proteomes:UP000032320};
RX   PubMed=25908145;
RA   Pal M., Swarnkar M.K., Thakur R., Kiran S., Chhibber S., Singh A.K.,
RA   Gulati A.;
RT   "Complete Genome Sequence of Paenibacillus sp. Strain IHBB 10380 Using
RT   PacBio Single-Molecule Real-Time Sequencing Technology.";
RL   Genome Announc. 3:0-0(2015).
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; CP010976; AJS58395.1; -; Genomic_DNA.
DR   RefSeq; WP_044876804.1; NZ_CP010976.1.
DR   AlphaFoldDB; A0A0D3V8K0; -.
DR   STRING; 1566358.UB51_07660; -.
DR   KEGG; pih:UB51_07660; -.
DR   PATRIC; fig|1566358.3.peg.1660; -.
DR   HOGENOM; CLU_010186_7_1_9; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000032320; 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; 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.
PE   3: Inferred from homology;
KW   Magnesium {ECO:0000256|RuleBase:RU365090};
KW   Metal-binding {ECO:0000256|RuleBase:RU365090};
KW   Molybdenum {ECO:0000256|ARBA:ARBA00022505, ECO:0000256|RuleBase:RU365090};
KW   Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150,
KW   ECO:0000256|RuleBase:RU365090};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032320};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          198..336
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   427 AA;  46752 MW;  F8DF04796188A86F CRC64;
     MEHSLDHSKF QRKAIQVNEA QNRIASYIHP IDIESVDLQA SHGRTLAQTI TAPHPYPSFR
     RSSMDGYAIC STDTIQCSSE AEITIWLEVI DDIPCGLVSS KTIIPGTTAR IMTGAQVPEG
     ADAVVMFEMV ELREENGIKL AGLRRHIEQG KNITPIGLEL QAEEEVLKQG VTIAAGEISV
     LATFGIHSVQ VYRRPRVAIF STGSELLKID EPLQSGKIRN SNTYMIASQV LEAGGEPVIL
     DAIMDDLSLA QRKVEEALAQ YDMVVTSGGV SVGDYDIMGD LVRSDRVTML YNKVTMRPGS
     VSTAAVKDNK CLFALSGNPG ACFVGFELFV RPSIRMMMLD PNPYLPEWTA TLGADYDKVN
     NFTRFVRAKI QIKEGVVYAT PTGVDESGVM ITIKDSDCLI IVPPSQEGLQ AGVKVKIMVL
     KNFIHPF
//
DBGET integrated database retrieval system