UniProt: B7S2W1

Database: UniProt
Entry: B7S2W1_9GAMM

LinkDB:  B7S2W1_9GAMM 
Original site:  B7S2W1_9GAMM

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

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ID   B7S2W1_9GAMM            Unreviewed;       397 AA.
AC   B7S2W1;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   ORFNames=GPB2148_1130 {ECO:0000313|EMBL:EEB77007.1};
OS   marine gamma proteobacterium HTCC2148.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae.
OX   NCBI_TaxID=247634 {ECO:0000313|EMBL:EEB77007.1, ECO:0000313|Proteomes:UP000002793};
RN   [1] {ECO:0000313|Proteomes:UP000002793}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2148 {ECO:0000313|Proteomes:UP000002793};
RX   PubMed=20472793; DOI=10.1128/jb.00511-10;
RA   Thrash J.C., Cho J.C., Ferriera S., Johnson J., Vergin K.L.,
RA   Giovannoni S.J.;
RT   "Genome sequences of strains HTCC2148 and HTCC2080, belonging to the
RT   OM60/NOR5 clade of the Gammaproteobacteria.";
RL   J. Bacteriol. 192:3842-3843(2010).
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}.
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DR   EMBL; DS999241; EEB77007.1; -; Genomic_DNA.
DR   AlphaFoldDB; B7S2W1; -.
DR   STRING; 247634.GPB2148_1130; -.
DR   eggNOG; COG0303; Bacteria.
DR   HOGENOM; CLU_010186_7_0_6; -.
DR   OrthoDB; 9804758at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000002793; 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: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.
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:UP000002793};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          172..310
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   397 AA;  40836 MW;  56CC38CF4959A6C8 CRC64;
     MPLEEALERI LGGARPTGAT DELSLIDALG AVLAEDVISG IDVPGDDNSA MDGYAVRGED
     LPGPLPISQR IAAGAVGEPL QPGTAARIFT GAPIPAGADA VVMQENCSVD QGGLLSVEGT
     VTTAQNIRPR GQDIAAGAVA LSKGRRLRPQ DLGLLASVGV ARVTVFRRLK VAVLSTGDEL
     IEPGTADLAG GQLYNSNRFT IAGLLARLGL EFVDVGIIPD DAQATAKALL RASELADCVI
     TSGGVSVGEE DHVKAQVEQI GHIDLWKLAI KPGKPLAFGA IGDTPFIGLP GNPTSVFATF
     CLVARPFLLK LQGATDCRIP ELTVTAGFAT AKSSPRQDHV RVSLESGDEG LVARRFANQS
     SGVLSSVSQS DALAVVPPGV VVSEGDKVQV LLLDLLA
//

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