ID Q6FB32_ACIAD Unreviewed; 307 AA.
AC Q6FB32;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 120.
DE SubName: Full=Bifunctional protein {ECO:0000313|EMBL:CAG68731.1};
GN Name=moaCB {ECO:0000313|EMBL:CAG68731.1};
GN OrderedLocusNames=ACIAD1903 {ECO:0000313|EMBL:CAG68731.1};
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977 {ECO:0000313|EMBL:CAG68731.1, ECO:0000313|Proteomes:UP000000430};
RN [1] {ECO:0000313|EMBL:CAG68731.1, ECO:0000313|Proteomes:UP000000430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1 {ECO:0000313|Proteomes:UP000000430};
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005046}.
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DR EMBL; CR543861; CAG68731.1; -; Genomic_DNA.
DR RefSeq; WP_004927103.1; NC_005966.1.
DR AlphaFoldDB; Q6FB32; -.
DR STRING; 202950.GCA_001485005_00460; -.
DR GeneID; 45234272; -.
DR KEGG; aci:ACIAD1903; -.
DR eggNOG; COG0315; Bacteria.
DR eggNOG; COG0521; Bacteria.
DR HOGENOM; CLU_063423_1_1_6; -.
DR OMA; TIYKTGV; -.
DR OrthoDB; 9794429at2; -.
DR BioCyc; ASP62977:ACIAD_RS08765-MONOMER; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000000430; Chromosome.
DR GO; GO:0061799; F:cyclic pyranopterin monophosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00886; MogA_MoaB; 1.
DR Gene3D; 3.40.980.10; MoaB/Mog-like domain; 1.
DR Gene3D; 3.30.70.640; Molybdopterin cofactor biosynthesis C (MoaC) domain; 1.
DR InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR InterPro; IPR001453; MoaB/Mog_dom.
DR InterPro; IPR012247; MoaC_MogA.
DR InterPro; IPR036522; MoaC_sf.
DR InterPro; IPR002820; Mopterin_CF_biosynth-C_dom.
DR NCBIfam; TIGR00177; molyb_syn; 1.
DR PANTHER; PTHR43764; MOLYBDENUM COFACTOR BIOSYNTHESIS; 1.
DR PANTHER; PTHR43764:SF1; MOLYBDOPTERIN MOLYBDENUMTRANSFERASE; 1.
DR Pfam; PF01967; MoaC; 1.
DR Pfam; PF00994; MoCF_biosynth; 1.
DR PIRSF; PIRSF036594; MoaC_MogA; 1.
DR SMART; SM00852; MoCF_biosynth; 1.
DR SUPFAM; SSF55040; Molybdenum cofactor biosynthesis protein C, MoaC; 1.
DR SUPFAM; SSF53218; Molybdenum cofactor biosynthesis proteins; 1.
PE 4: Predicted;
KW Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150};
KW Reference proteome {ECO:0000313|Proteomes:UP000000430}.
FT DOMAIN 151..293
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 307 AA; 33262 MW; F119230B5F9EC934 CRC64;
MKNVGMKPES YRIAEAQAIL YAPPHCIELL RTGNTEKGDA LKTGRIAGIL AAKRTDELIP
LCHPLPIYRA EVEYELHENF VEILTTVETI GPTGVEMEAL TAASIAGLTL YDMLKPHCEP
EDLVLDQCKL LKKKGGKSHF KRTLRQAVSA AVIVLSDTVA SGKKPDTAGK SVVDTLNEAG
FTPIHYQILP DESDQLKDLV LELTQSYACI ITVGGTGIGK RDITVDTLEP LLERKLDGLM
EAARAFGQRR TPYAAMSRGV AGFIDRSLIM TLPGSRGGAS ESMAALLPAI VHIFDVCRDL
PHPGGYE
//