ID A0A1S1V3W2_9FIRM Unreviewed; 461 AA.
AC A0A1S1V3W2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00187, ECO:0000256|HAMAP-Rule:MF_00316};
DE Includes:
DE RecName: Full=Probable molybdenum cofactor guanylyltransferase {ECO:0000256|HAMAP-Rule:MF_00316};
DE Short=MoCo guanylyltransferase {ECO:0000256|HAMAP-Rule:MF_00316};
DE EC=2.7.7.77 {ECO:0000256|HAMAP-Rule:MF_00316};
DE AltName: Full=GTP:molybdopterin guanylyltransferase {ECO:0000256|HAMAP-Rule:MF_00316};
DE AltName: Full=Molybdopterin-guanine dinucleotide synthase {ECO:0000256|HAMAP-Rule:MF_00316};
DE Short=MGD synthase {ECO:0000256|HAMAP-Rule:MF_00316};
DE AltName: Full=Molybdopterin guanylyltransferase {ECO:0000256|HAMAP-Rule:MF_00316};
DE AltName: Full=Mo-MPT guanylyltransferase {ECO:0000256|HAMAP-Rule:MF_00316};
DE Includes:
DE RecName: Full=Sulfur carrier protein FdhD {ECO:0000256|HAMAP-Rule:MF_00187};
GN Name=mobA {ECO:0000256|HAMAP-Rule:MF_00316,
GN ECO:0000313|EMBL:OHW61343.1};
GN Synonyms=fdhD {ECO:0000256|HAMAP-Rule:MF_00187};
GN ORFNames=EUAN_22860 {ECO:0000313|EMBL:OHW61343.1};
OS Andreesenia angusta.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Gottschalkiaceae;
OC Andreesenia.
OX NCBI_TaxID=39480 {ECO:0000313|EMBL:OHW61343.1, ECO:0000313|Proteomes:UP000180254};
RN [1] {ECO:0000313|EMBL:OHW61343.1, ECO:0000313|Proteomes:UP000180254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1989 {ECO:0000313|EMBL:OHW61343.1,
RC ECO:0000313|Proteomes:UP000180254};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Eubacterium angustum.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for formate dehydrogenase (FDH) activity. Acts as a
CC sulfur carrier protein that transfers sulfur from IscS to the
CC molybdenum cofactor prior to its insertion into FDH.
CC {ECO:0000256|HAMAP-Rule:MF_00187}.
CC -!- FUNCTION: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT)
CC cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine
CC dinucleotide (Mo-MGD) cofactor. {ECO:0000256|HAMAP-Rule:MF_00316}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin
CC guanine dinucleotide; Xref=Rhea:RHEA:34243, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:71302,
CC ChEBI:CHEBI:71310; EC=2.7.7.77; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00316};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00316};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00316}.
CC -!- DOMAIN: The N-terminal domain determines nucleotide recognition and
CC specific binding, while the C-terminal domain determines the specific
CC binding to the target protein. {ECO:0000256|HAMAP-Rule:MF_00316}.
CC -!- SIMILARITY: Belongs to the FdhD family. {ECO:0000256|HAMAP-
CC Rule:MF_00187}.
CC -!- SIMILARITY: Belongs to the MobA family. {ECO:0000256|HAMAP-
CC Rule:MF_00316}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00316}.
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:OHW61343.1}.
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DR EMBL; MKIE01000015; OHW61343.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S1V3W2; -.
DR STRING; 39480.EUAN_22860; -.
DR OrthoDB; 9782042at2; -.
DR Proteomes; UP000180254; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061603; F:molybdenum cofactor guanylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0097163; F:sulfur carrier activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016783; F:sulfurtransferase activity; IEA:InterPro.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd02503; MobA; 1.
DR Gene3D; 3.10.20.10; -; 1.
DR Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR HAMAP; MF_00187; FdhD; 1.
DR HAMAP; MF_00316; MobA; 1.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR InterPro; IPR003786; FdhD.
DR InterPro; IPR025877; MobA-like_NTP_Trfase.
DR InterPro; IPR013482; Molybde_CF_guanTrfase.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR NCBIfam; TIGR00129; fdhD_narQ; 1.
DR PANTHER; PTHR30592; FORMATE DEHYDROGENASE; 1.
DR PANTHER; PTHR30592:SF1; SULFUR CARRIER PROTEIN FDHD; 1.
DR Pfam; PF02634; FdhD-NarQ; 1.
DR Pfam; PF12804; NTP_transf_3; 1.
DR SUPFAM; SSF53927; Cytidine deaminase-like; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00316};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00316}; Magnesium {ECO:0000256|HAMAP-Rule:MF_00316};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00316};
KW Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150,
KW ECO:0000256|HAMAP-Rule:MF_00316};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00316}; Nucleotidyltransferase {ECO:0000313|EMBL:OHW61343.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000180254};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00316, ECO:0000313|EMBL:OHW61343.1}.
FT DOMAIN 9..161
FT /note="MobA-like NTP transferase"
FT /evidence="ECO:0000259|Pfam:PF12804"
FT ACT_SITE 305
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00187"
FT BINDING 12..14
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00316"
FT BINDING 24
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00316"
FT BINDING 69
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00316"
FT BINDING 98
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00316"
FT BINDING 98
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00316"
FT BINDING 443..448
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00187"
SQ SEQUENCE 461 AA; 52090 MW; 0F1BEEC5815A2D6F CRC64;
MGENKFGTAV ILAGGKSSRM GFNKEFLEID GESLVKKNIE KLKTIFNEII VVTNNPEYYE
SLNIITVQDI YFQKGPLSGI HASLKRSSSE YIYLLACDMP EIDIPFIKWM MDIVKREAPE
ISVVRRDGRI EPFNGFYSVA LADRVEELLK HDKLAIRALM SEAKVEFIDL HEVQSGRDIF
LNLNTQEDLH GYLEQRRDTV MKVVSKRDVL KIRYDDSAVE EDSIITEYPF TVFLNGKEFL
TLLCTKQSLD YLLVGFLISE GLIDGKQDIE KLEIDEEKGT GYVETVKKSN LMEKLYGKRT
LTSGCGKGTV FYSVVDSFKS KKVDQDFKLD VDSMKDLMRK FNRYSETFLE TGGVHSCALS
DGEDIAVFAD DIGRHNALDK IIGEAVMKDI EFDDKVVVTT GRISSEIMIK IAKRGIPAIV
SKSAPTQLAI EIAEDLGITV VGFARGQKMN IYTNIDRYIQ L
//
