GenomeNet

Database: UniProt
Entry: A0A0P9CXV7_9CHLR
LinkDB: A0A0P9CXV7_9CHLR
Original site: A0A0P9CXV7_9CHLR 
ID   A0A0P9CXV7_9CHLR        Unreviewed;       218 AA.
AC   A0A0P9CXV7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   13-SEP-2023, entry version 20.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
DE   Flags: Fragment;
GN   ORFNames=SE17_41205 {ECO:0000313|EMBL:KPV47854.1};
OS   Kouleothrix aurantiaca.
OC   Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Roseiflexineae;
OC   Roseiflexaceae; Kouleothrix.
OX   NCBI_TaxID=186479 {ECO:0000313|EMBL:KPV47854.1, ECO:0000313|Proteomes:UP000050509};
RN   [1] {ECO:0000313|EMBL:KPV47854.1, ECO:0000313|Proteomes:UP000050509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COM-B {ECO:0000313|EMBL:KPV47854.1,
RC   ECO:0000313|Proteomes:UP000050509};
RA   Hemp J.;
RT   "Draft genome sequence of Kouleothrix aurantiaca JCM 19913.";
RL   Submitted (SEP-2015) 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|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;
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|ARBA:ARBA00005046, ECO:0000256|RuleBase:RU365090}.
CC   -!- SIMILARITY: Belongs to the MoeA family.
CC       {ECO:0000256|RuleBase:RU365090}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPV47854.1}.
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; LJCR01003169; KPV47854.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P9CXV7; -.
DR   PATRIC; fig|186479.3.peg.6622; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000050509; Unassembled WGS sequence.
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   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   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   SMART; SM00852; MoCF_biosynth; 1.
DR   SUPFAM; SSF63867; MoeA C-terminal domain-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:UP000050509};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          1..130
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KPV47854.1"
SQ   SEQUENCE   218 AA;  23068 MW;  568FE22E377BF00B CRC64;
     VYEPGLSIPP GGIRDSNRYA LMAAAREAGC ETMSLGIARD DVQVQREAIR DGLARADVLL
     TSGGVSMGTR DLIKPLLAEL GTVHFGRIAF KPGKPTTFAT IGEKLLFGLP GFPVSSLVSF
     EVFVRPALRR LQGDAHPERA QVRVALASQI VAAPDRPEYQ RAIVSWEGGR LVARGTGAQG
     SSRLLSMRGA NALLLVPGDG QTYPPGAELD ALLTGPIE
//
DBGET integrated database retrieval system