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Database: UniProt
Entry: A0A024HJW8_PSEKB
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ID   A0A024HJW8_PSEKB        Unreviewed;       404 AA.
AC   A0A024HJW8;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   Name=moeA {ECO:0000313|EMBL:CDF85141.1};
GN   ORFNames=PKB_3803 {ECO:0000313|EMBL:CDF85141.1};
OS   Pseudomonas knackmussii (strain DSM 6978 / LMG 23759 / B13).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1301098 {ECO:0000313|EMBL:CDF85141.1, ECO:0000313|Proteomes:UP000025241};
RN   [1] {ECO:0000313|EMBL:CDF85141.1, ECO:0000313|Proteomes:UP000025241}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B13 {ECO:0000313|EMBL:CDF85141.1,
RC   ECO:0000313|Proteomes:UP000025241};
RA   Linke B.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDF85141.1, ECO:0000313|Proteomes:UP000025241}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B13 {ECO:0000313|EMBL:CDF85141.1,
RC   ECO:0000313|Proteomes:UP000025241};
RA   Miyazaki R., Bertelli C., Falquet L., Robinson-Rechavi M., Gharib W.,
RA   Roy S., Van der Meer J.R.;
RT   "Genome sequence of the 3-chlorobenzoate degrading bacterium Pseudomonas
RT   knackmussii B13 shows multiple evidence for horizontal gene transfer.";
RL   Submitted (MAY-2014) 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}.
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DR   EMBL; HG322950; CDF85141.1; -; Genomic_DNA.
DR   RefSeq; WP_043253504.1; NZ_HG322950.1.
DR   AlphaFoldDB; A0A024HJW8; -.
DR   STRING; 1301098.PKB_3803; -.
DR   KEGG; pkc:PKB_3803; -.
DR   PATRIC; fig|1301098.3.peg.3813; -.
DR   eggNOG; COG0303; Bacteria.
DR   HOGENOM; CLU_010186_7_0_6; -.
DR   OMA; MTGAMVP; -.
DR   OrthoDB; 9804758at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000025241; 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; 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:UP000025241};
KW   Transferase {ECO:0000256|RuleBase:RU365090, ECO:0000313|EMBL:CDF85141.1}.
FT   DOMAIN          184..320
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   404 AA;  43200 MW;  CFEAE84B6BF57C48 CRC64;
     MSGCDKPGLL PVEEALERLL DLARQTPINE VERVSLGEAD GRVLAEPLLS GLDLPPWDNS
     AMDGYALRLA DWQGEPMAVS QKIFAGVAPE ALQLGTCARI FTGAPLPQGA DCVEMQENVE
     VLADGRVRFL QPLKFGQHVR PQGQETLKGE CVLPAGTRLG AIELGLAASL GQAELSVRRK
     PRVALLSTGD ELVEPGKPLA LGQIYNSNRA LLKAWLLRSG CEVVDAGILP DDLAKTCEVL
     GSLAGVDLIL STGGVSVGEA DFLGAALREA GELSLWKLAI KPGKPLTVGH YQGVPVIGLP
     GNPASTLVTF ALLARPYLLR RLGVEEVAPL RFEVPAGFAW KHAGNRREYL RARLENGRAL
     LYPNQSSGVL RSAAWADGLV EVREGRTLEE GEMLPFIPLS EVLN
//
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