ID A0A0D8HGD5_9ACTN Unreviewed; 406 AA.
AC A0A0D8HGD5;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
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:KJF16983.1};
GN ORFNames=AXFE_21860 {ECO:0000313|EMBL:KJF16983.1};
OS Acidithrix ferrooxidans.
OC Bacteria; Actinomycetota; Acidimicrobiia; Acidimicrobiales;
OC Acidimicrobiaceae; Acidithrix.
OX NCBI_TaxID=1280514 {ECO:0000313|EMBL:KJF16983.1, ECO:0000313|Proteomes:UP000032360};
RN [1] {ECO:0000313|EMBL:KJF16983.1, ECO:0000313|Proteomes:UP000032360}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Py-F3 {ECO:0000313|EMBL:KJF16983.1,
RC ECO:0000313|Proteomes:UP000032360};
RA Poehlein A., Eisen S., Schloemann M., Johnson B.D., Daniel R., Muehling M.;
RT "Draft genome of the acidophilic iron oxidizer Acidithrix ferrooxidans
RT strain Py-F3.";
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:KJF16983.1}.
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DR EMBL; JXYS01000069; KJF16983.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D8HGD5; -.
DR STRING; 1280514.AXFE_21860; -.
DR PATRIC; fig|1280514.3.peg.2854; -.
DR OrthoDB; 3196725at2; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000032360; 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; 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.
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:UP000032360};
KW Transferase {ECO:0000256|RuleBase:RU365090, ECO:0000313|EMBL:KJF16983.1}.
FT DOMAIN 179..318
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 406 AA; 43234 MW; 5C49350439ED04AB CRC64;
MIPLTQAQQY VLSNIDTSRA MAIPIDEANG LITSGSLEAM EEIPPFDNTA VDGIAIRSEE
IDRLNLSGSI EVRIAATIAA GSPDKVEIAP GTCVRIMTGA PIPSNCSAVV MIEDVVASDI
MATISCRIAP GDNIRRKGSD IAIGTRLFES NTRLTPAHIG VLASVGFAKV PAFRRIKIGV
ISTGDELAEV GQALTYGKIR DSNRHSLLAI ASSSGANVLD LGIVKDRPED LRKAFLDAAK
EVDVIITSGG VSVGDFDYTK AILNELSNGK AQWMQIAIRP AKPFAFGKID NTPFFGLPGN
PVSALVSFEL LVKPALRKMQ GDLEPLPRPV LAKATGAYKR TPDGKRHFVR SNLHVNNSGA
LAVKPLDKQG SHMLHEMSKA NSLIIVEDGD GFLKDQEVEV LPLGAL
//
