UniProt: A0A0M2KCL8

Database: UniProt
Entry: A0A0M2KCL8_9GAMM

LinkDB:  A0A0M2KCL8_9GAMM 
Original site:  A0A0M2KCL8_9GAMM

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (13)   
   InterPro (8)   
   Pfam (3)   
   PROSITE (1)   
   SMART (1)   
All databases (19)   

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ID   A0A0M2KCL8_9GAMM        Unreviewed;       412 AA.
AC   A0A0M2KCL8;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   ORFNames=SY86_05550 {ECO:0000313|EMBL:KKF35012.1};
OS   Erwinia tracheiphila.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=65700 {ECO:0000313|EMBL:KKF35012.1, ECO:0000313|Proteomes:UP000033924};
RN   [1] {ECO:0000313|EMBL:KKF35012.1, ECO:0000313|Proteomes:UP000033924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BuffGH {ECO:0000313|EMBL:KKF35012.1,
RC   ECO:0000313|Proteomes:UP000033924};
RA   Shapiro L.R.;
RT   "Erwinia tracheiphila.";
RL   Submitted (JAN-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|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   -!- 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:KKF35012.1}.
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DR   EMBL; JXNU01000003; KKF35012.1; -; Genomic_DNA.
DR   RefSeq; WP_016189716.1; NZ_JXNU01000003.1.
DR   AlphaFoldDB; A0A0M2KCL8; -.
DR   STRING; 65700.SY86_05550; -.
DR   PATRIC; fig|65700.7.peg.1401; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000033924; 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   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; 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; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 1.
DR   PANTHER; PTHR10192:SF34; MOLYBDOPTERIN MOLYBDENUMTRANSFERASE; 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.
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:UP000033924};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          182..319
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   412 AA;  44101 MW;  165A9AFF18986140 CRC64;
     METFTAGLIS LDDALSTMLC RIVPLTQTET LPLTAAGGRI TARPTISPVQ VPPFDNAAMD
     GYAVRLHDVQ SGQPLSVAGK TFAGAPWRDL WPVGSCIRIM TGAPLPDGTE AVVMQEETCL
     VNDQVKINTD VVYGQNIRLA GEDIAAGARV LDKGVRLGTA ELPLLASLGV AEIEVIRRVR
     VAIFSTGNEL QPIGKALADG QIYDTNRLAV QLMLNKLGCE VIDLGIIADD PQTLRAAFLQ
     ADREADVVIS SGGVSVGEAD YTKAMLEELG EIAFWKLAIK PGKPFAFGRL KHSWFCGLPG
     NPVSATLTFY QLVQPVLTRL AGQKASALPA RQRVRAADAL KKKLGQLDFQ RGLLLPDASG
     ELQVHTTGPQ GSHVFSSFSQ ANCFIVLERE RGNVAAGEWV DVEPFNSLLA GY
//

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