PAOD_ECOLI
ID PAOD_ECOLI Reviewed; 318 AA.
AC P77183; Q2MCD9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Molybdenum cofactor insertion chaperone PaoD {ECO:0000305};
GN Name=paoD {ECO:0000303|PubMed:21081498}; Synonyms=yagQ;
GN OrderedLocusNames=b0283, JW0277;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19368556; DOI=10.1111/j.1742-4658.2009.07000.x;
RA Neumann M., Mittelstaedt G., Iobbi-Nivol C., Saggu M., Lendzian F.,
RA Hildebrandt P., Leimkuehler S.;
RT "A periplasmic aldehyde oxidoreductase represents the first molybdopterin
RT cytosine dinucleotide cofactor containing molybdo-flavoenzyme from
RT Escherichia coli.";
RL FEBS J. 276:2762-2774(2009).
RN [5]
RP FUNCTION, INTERACTION WITH MOCA, AND NOMENCLATURE.
RX PubMed=21081498; DOI=10.1074/jbc.m110.155671;
RA Neumann M., Seduk F., Iobbi-Nivol C., Leimkuhler S.;
RT "Molybdopterin dinucleotide biosynthesis in Escherichia coli:
RT identification of amino acid residues of molybdopterin dinucleotide
RT transferases that determine specificity for binding of guanine or cytosine
RT nucleotides.";
RL J. Biol. Chem. 286:1400-1408(2011).
RN [6]
RP FUNCTION, SUBUNIT, AND CRYSTALLIZATION.
RX PubMed=24498065; DOI=10.1371/journal.pone.0087295;
RA Otrelo-Cardoso A.R., Schwuchow V., Rodrigues D., Cabrita E.J.,
RA Leimkuehler S., Romao M.J., Santos-Silva T.;
RT "Biochemical, stabilization and crystallization studies on a molecular
RT chaperone (PaoD) involved in the maturation of molybdoenzymes.";
RL PLoS ONE 9:E87295-E87295(2014).
CC -!- FUNCTION: Chaperone required for the production of an active PaoABC
CC aldehyde oxidoreductase. Stabilizes the PaoC subunit and is required
CC for the insertion of the molybdenum cofactor into this subunit
CC (PubMed:19368556, PubMed:21081498). Binds molybdenum cofactor. Binds
CC the molybdopterin cytosine dinucleotide (MCD) form of the cofactor
CC after its formation by the molybdenum cofactor cytidylyltransferase
CC MocA (PubMed:24498065). {ECO:0000269|PubMed:19368556,
CC ECO:0000269|PubMed:21081498, ECO:0000269|PubMed:24498065}.
CC -!- SUBUNIT: Homodimer in solution (PubMed:24498065). Interacts with MocA
CC (PubMed:21081498). {ECO:0000269|PubMed:21081498,
CC ECO:0000269|PubMed:24498065}.
CC -!- DISRUPTION PHENOTYPE: Mutation results in complete impairment of cell
CC growth in the presence of cinnamaldehyde.
CC {ECO:0000269|PubMed:19368556}.
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DR EMBL; U73857; AAB18012.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73386.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76067.1; -; Genomic_DNA.
DR PIR; C64754; C64754.
DR RefSeq; NP_414817.1; NC_000913.3.
DR RefSeq; WP_000121359.1; NZ_SSZK01000048.1.
DR AlphaFoldDB; P77183; -.
DR SMR; P77183; -.
DR BioGRID; 4261499; 12.
DR IntAct; P77183; 4.
DR STRING; 511145.b0283; -.
DR PaxDb; P77183; -.
DR PRIDE; P77183; -.
DR EnsemblBacteria; AAC73386; AAC73386; b0283.
DR EnsemblBacteria; BAE76067; BAE76067; BAE76067.
DR GeneID; 945010; -.
DR KEGG; ecj:JW0277; -.
DR KEGG; eco:b0283; -.
DR PATRIC; fig|1411691.4.peg.1995; -.
DR EchoBASE; EB3326; -.
DR eggNOG; COG1975; Bacteria.
DR HOGENOM; CLU_041115_2_1_6; -.
DR InParanoid; P77183; -.
DR OMA; EDDLSWG; -.
DR PhylomeDB; P77183; -.
DR BioCyc; EcoCyc:G6154-MON; -.
DR BioCyc; MetaCyc:G6154-MON; -.
DR SABIO-RK; P77183; -.
DR PRO; PR:P77183; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IDA:EcoCyc.
DR InterPro; IPR003777; XdhC_CoxI.
DR InterPro; IPR027051; XdhC_Rossmann_dom.
DR Pfam; PF13478; XdhC_C; 1.
DR Pfam; PF02625; XdhC_CoxI; 1.
PE 1: Evidence at protein level;
KW Chaperone; Reference proteome.
FT CHAIN 1..318
FT /note="Molybdenum cofactor insertion chaperone PaoD"
FT /id="PRO_0000168562"
SQ SEQUENCE 318 AA; 34954 MW; BCE8A8A8DD78D55A CRC64;
MSYPLFDKDE HWHKPEQAFL TDDHRTILRF AVEALMSGKG AVLVTLVEIR GGAARPLGAQ
MVVREDGRYC GFVSGGCVEA AAAFEALEMM GSGRDREIRY GEGSPWFDIV LPCGGGITLT
LHKLRSAQPL LAVLNRLEQR KPVGLRYDPQ AQSLVCLPTQ TRTGWNLNGF EVGFRPCVRL
MIYGRSLEAQ ATASLAAATG YDSHIFDLFP ASASAQIDTD TAVILLCHDL NRELPVLQAA
REAKPFYLGA LGSYRTHTLR LQKLHELGWS REETTQIRAP VGIFPKARDA HTLALSVLAE
VASVRLHQEE DSCLPPSS
