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Database: UniProt
Entry: Q3AEF7_CARHZ
LinkDB: Q3AEF7_CARHZ
Original site: Q3AEF7_CARHZ 
ID   Q3AEF7_CARHZ            Unreviewed;       338 AA.
AC   Q3AEF7;
DT   22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2005, sequence version 1.
DT   24-JAN-2024, entry version 78.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   OrderedLocusNames=CHY_0621 {ECO:0000313|EMBL:ABB15537.1};
OS   Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 /
OS   Z-2901).
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Carboxydothermus.
OX   NCBI_TaxID=246194 {ECO:0000313|EMBL:ABB15537.1, ECO:0000313|Proteomes:UP000002706};
RN   [1] {ECO:0000313|EMBL:ABB15537.1, ECO:0000313|Proteomes:UP000002706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-161 / DSM 6008 / Z-2901
RC   {ECO:0000313|Proteomes:UP000002706};
RX   PubMed=16311624; DOI=10.1371/journal.pgen.0010065;
RA   Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J.,
RA   Madupu R., Sullivan S.A., Kolonay J.F., Haft D.H., Nelson W.C.,
RA   Tallon L.J., Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B.,
RA   Robb F.T., Eisen J.A.;
RT   "Life in hot carbon monoxide: the complete genome sequence of
RT   Carboxydothermus hydrogenoformans Z-2901.";
RL   PLoS Genet. 1:563-574(2005).
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|RuleBase:RU365090}.
CC   -!- SIMILARITY: Belongs to the MoeA family.
CC       {ECO:0000256|RuleBase:RU365090}.
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DR   EMBL; CP000141; ABB15537.1; -; Genomic_DNA.
DR   RefSeq; WP_011343553.1; NC_007503.1.
DR   AlphaFoldDB; Q3AEF7; -.
DR   STRING; 246194.CHY_0621; -.
DR   KEGG; chy:CHY_0621; -.
DR   eggNOG; COG0303; Bacteria.
DR   HOGENOM; CLU_068847_1_0_9; -.
DR   InParanoid; Q3AEF7; -.
DR   OMA; LNGADWV; -.
DR   OrthoDB; 9767940at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000002706; 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; cd03522; MoeA_like; 1.
DR   Gene3D; 3.40.980.10; MoaB/Mog-like domain; 1.
DR   InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR   InterPro; IPR001453; MoaB/Mog_dom.
DR   InterPro; IPR038987; MoeA-like.
DR   PANTHER; PTHR10192; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 1.
DR   PANTHER; PTHR10192:SF28; MOLYBDOPTERIN MOLYBDENUMTRANSFERASE; 1.
DR   Pfam; PF00994; MoCF_biosynth; 1.
DR   SMART; SM00852; MoCF_biosynth; 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:UP000002706};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          173..305
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   338 AA;  37021 MW;  A4CC1236A3BF9073 CRC64;
     MKKVPVQEAI GMVLCHDITK IVPGEFKGPA FKKGHIIREE DIPELLKLGK DHIYVWEVKE
     GILHENEAAQ RIARAVGGDR FIFTEPKEGK VNLLVKERGL FKVDREALFE INMLGELMVS
     TLHTNRVVGP GQYVAGTRII PLVIEEEKIK KVEEICRDKK VLEVKPLAQP KVGVVNTGNE
     IFYGRIEDKF TPVLAEKLKA FGLTIDMHLK APDDVEKIAE AILKLKEAGM ELILATGGMS
     VDPDDLTPGG IKRAGGEVVV YGSPVLPGAM FLYALLDGVP VLGLPGCVMY SKTTIFDLVL
     PRILAGEVLT RKDIAALGHG GLCLECPVCT YPHCPFGK
//
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