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Database: UniProt
Entry: K4LIS7_THEPS
LinkDB: K4LIS7_THEPS
Original site: K4LIS7_THEPS 
ID   K4LIS7_THEPS            Unreviewed;       397 AA.
AC   K4LIS7;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 42.
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   Name=moeA5 {ECO:0000313|EMBL:AFV12896.1};
GN   OrderedLocusNames=Tph_c27310 {ECO:0000313|EMBL:AFV12896.1};
OS   Thermacetogenium phaeum (strain ATCC BAA-254 / DSM 26808 / PB).
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermacetogenium.
OX   NCBI_TaxID=1089553 {ECO:0000313|EMBL:AFV12896.1, ECO:0000313|Proteomes:UP000000467};
RN   [1] {ECO:0000313|EMBL:AFV12896.1, ECO:0000313|Proteomes:UP000000467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-254 / DSM 26808 / PB
RC   {ECO:0000313|Proteomes:UP000000467};
RX   PubMed=23259483; DOI=10.1186/1471-2164-13-723;
RA   Oehler D., Poehlein A., Leimbach A., Muller N., Daniel R., Gottschalk G.,
RA   Schink B.;
RT   "Genome-guided analysis of physiological and morphological traits of the
RT   fermentative acetate oxidizer Thermacetogenium phaeum.";
RL   BMC Genomics 13:723-723(2012).
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; CP003732; AFV12896.1; -; Genomic_DNA.
DR   RefSeq; WP_015051755.1; NZ_KI912609.1.
DR   AlphaFoldDB; K4LIS7; -.
DR   STRING; 1089553.Tph_c27310; -.
DR   KEGG; tpz:Tph_c27310; -.
DR   eggNOG; COG0303; Bacteria.
DR   HOGENOM; CLU_010186_7_1_9; -.
DR   OMA; VDHVHPT; -.
DR   OrthoDB; 9804758at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000000467; 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   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|RuleBase:RU365090};
KW   Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150,
KW   ECO:0000256|RuleBase:RU365090};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000467};
KW   Transferase {ECO:0000256|RuleBase:RU365090, ECO:0000313|EMBL:AFV12896.1}.
FT   DOMAIN          176..311
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   397 AA;  42026 MW;  0790F6B0ADBA345F CRC64;
     MKSCLPLEDS QELLLSSIKP LLSETITLEE APGRVLAADI FAPHDLPPYP QAALDGFAIP
     REGKRGSPLS VKRILGAGDL PGHPLGPGEA AGVLTGGHIP PGTAAVVRQE DAMVKDGILT
     IDKDLTVGEN IRDQGEDFPA GAVIARRGTR ITPGLSAVLA AFGFQEISVF RRPRVAIVNL
     GKEIAPHQAT PLPGQVRDSN GPLLAALTRR TGGQVVAIHY ARTKTEKQIG ELLMEADVVL
     TIGGTASGNN DPGHHFIERV GGRPLFAGYQ VKPGSHTSAG ILDGRIILML SGNPVPCAVG
     YHLLAAPVLR ALQGLNPYLH RIPAVATNSF PKRGGPRRFL LGYALGSHQG WRVAVLPFQK
     PSNLHSLIDY NCLIDLPAGH PPLQLGDEVK IILLENA
//
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