PAOC_ECOLI
ID PAOC_ECOLI Reviewed; 732 AA.
AC P77489; Q2MCD8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Aldehyde oxidoreductase molybdenum-binding subunit PaoC {ECO:0000305};
DE EC=1.2.99.6 {ECO:0000269|PubMed:19368556, ECO:0000269|PubMed:21081498};
GN Name=paoC {ECO:0000303|PubMed:21081498}; Synonyms=yagR;
GN OrderedLocusNames=b0284, JW0278;
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, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, DISRUPTION
RP PHENOTYPE, ACTIVE SITE, AND MUTAGENESIS OF GLU-692.
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 CATALYTIC ACTIVITY, 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 CRYSTALLIZATION, AND SUBUNIT.
RX PubMed=24492481; DOI=10.3390/ijms15022223;
RA Otrelo-Cardoso A.R., da Silva Correia M.A., Schwuchow V., Svergun D.I.,
RA Romao M.J., Leimkuehler S., Santos-Silva T.;
RT "Structural data on the periplasmic aldehyde oxidoreductase PaoABC from
RT Escherichia coli: SAXS and preliminary X-ray crystallography analysis.";
RL Int. J. Mol. Sci. 15:2223-2236(2014).
RN [7] {ECO:0007744|PDB:5G5G, ECO:0007744|PDB:5G5H}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH MOLYBDOPTERIN
RP CYTOSINE DINUCLEOTIDE, COFACTOR, SUBUNIT, AND MUTAGENESIS OF ARG-440.
RX PubMed=27622978; DOI=10.1021/acschembio.6b00572;
RA Correia M.A., Otrelo-Cardoso A.R., Schwuchow V., Sigfridsson Clauss K.G.,
RA Haumann M., Romao M.J., Leimkuhler S., Santos-Silva T.;
RT "The Escherichia coli periplasmic aldehyde oxidoreductase is an exceptional
RT member of the xanthine oxidase family of molybdoenzymes.";
RL ACS Chem. Biol. 11:2923-2935(2016).
CC -!- FUNCTION: Oxidizes aldehydes to the corresponding carboxylic acids with
CC a preference for aromatic aldehydes. It might play a role in the
CC detoxification of aldehydes to avoid cell damage.
CC {ECO:0000269|PubMed:19368556}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + an aldehyde + H2O = a carboxylate + AH2 + H(+);
CC Xref=Rhea:RHEA:56856, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17478, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:29067; EC=1.2.99.6;
CC Evidence={ECO:0000269|PubMed:19368556, ECO:0000269|PubMed:21081498};
CC -!- COFACTOR:
CC Name=Mo-molybdopterin cytosine dinucleotide; Xref=ChEBI:CHEBI:71308;
CC Evidence={ECO:0000269|PubMed:19368556, ECO:0000269|PubMed:27622978};
CC -!- ACTIVITY REGULATION: The complex requires PaoD for activity.
CC {ECO:0000269|PubMed:19368556}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=63 uM for cinnamaldehyde {ECO:0000269|PubMed:19368556};
CC KM=70 uM for benzaldehyde {ECO:0000269|PubMed:19368556};
CC KM=132 uM for vanillin {ECO:0000269|PubMed:19368556};
CC Note=kcat is 84 sec(-1) with cinnamaldehyde as substrate. kcat is 97
CC sec(-1) with benzaldehyde as substrate. kcat is 125 sec(-1) with
CC vanillin as substrate. {ECO:0000269|PubMed:19368556};
CC pH dependence:
CC Stable up to a pH of 4. {ECO:0000269|PubMed:19368556};
CC -!- SUBUNIT: Heterotrimer composed of PaoA, PaoB and PaoC.
CC {ECO:0000269|PubMed:19368556, ECO:0000269|PubMed:24492481,
CC ECO:0000269|PubMed:27622978}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:19368556}.
CC -!- DISRUPTION PHENOTYPE: Mutation results in complete impairment of cell
CC growth in the presence of cinnamaldehyde.
CC {ECO:0000269|PubMed:19368556}.
CC -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; U73857; AAB18013.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73387.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76068.1; -; Genomic_DNA.
DR PIR; D64754; D64754.
DR RefSeq; NP_414818.1; NC_000913.3.
DR RefSeq; WP_000667026.1; NZ_SSZK01000048.1.
DR PDB; 5G5G; X-ray; 1.70 A; C=1-732.
DR PDB; 5G5H; X-ray; 2.30 A; C=1-732.
DR PDBsum; 5G5G; -.
DR PDBsum; 5G5H; -.
DR AlphaFoldDB; P77489; -.
DR SMR; P77489; -.
DR BioGRID; 4261492; 18.
DR ComplexPortal; CPX-4281; PaoABC periplasmic aldehyde oxidoreductase.
DR IntAct; P77489; 11.
DR STRING; 511145.b0284; -.
DR jPOST; P77489; -.
DR PaxDb; P77489; -.
DR PRIDE; P77489; -.
DR EnsemblBacteria; AAC73387; AAC73387; b0284.
DR EnsemblBacteria; BAE76068; BAE76068; BAE76068.
DR GeneID; 66671421; -.
DR GeneID; 944961; -.
DR KEGG; ecj:JW0278; -.
DR KEGG; eco:b0284; -.
DR PATRIC; fig|1411691.4.peg.1994; -.
DR EchoBASE; EB3327; -.
DR eggNOG; COG1529; Bacteria.
DR HOGENOM; CLU_001681_2_2_6; -.
DR InParanoid; P77489; -.
DR OMA; SWMRAPG; -.
DR PhylomeDB; P77489; -.
DR BioCyc; EcoCyc:G6155-MON; -.
DR BioCyc; MetaCyc:G6155-MON; -.
DR BRENDA; 1.17.1.4; 2026.
DR PRO; PR:P77489; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1990204; C:oxidoreductase complex; IPI:ComplexPortal.
DR GO; GO:0042597; C:periplasmic space; NAS:EcoCyc.
DR GO; GO:0047770; F:carboxylate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0030151; F:molybdenum ion binding; IDA:EcoCyc.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IDA:EcoCyc.
DR GO; GO:0019439; P:aromatic compound catabolic process; IDA:ComplexPortal.
DR GO; GO:0110095; P:cellular detoxification of aldehyde; IDA:ComplexPortal.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
DR InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
DR InterPro; IPR016208; Ald_Oxase/xanthine_DH.
DR InterPro; IPR008274; AldOxase/xan_DH_Mopterin-bd.
DR InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
DR PANTHER; PTHR11908; PTHR11908; 1.
DR Pfam; PF01315; Ald_Xan_dh_C; 1.
DR Pfam; PF02738; Ald_Xan_dh_C2; 1.
DR SMART; SM01008; Ald_Xan_dh_C; 1.
DR SUPFAM; SSF54665; SSF54665; 1.
DR SUPFAM; SSF56003; SSF56003; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Metal-binding; Molybdenum; Oxidoreductase; Periplasm;
KW Reference proteome.
FT CHAIN 1..732
FT /note="Aldehyde oxidoreductase molybdenum-binding subunit
FT PaoC"
FT /id="PRO_0000166090"
FT ACT_SITE 692
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:19368556"
FT BINDING 241..242
FT /ligand="Mo-molybdopterin cytosine dinucleotide"
FT /ligand_id="ChEBI:CHEBI:71308"
FT /evidence="ECO:0000269|PubMed:27622978,
FT ECO:0007744|PDB:5G5G, ECO:0007744|PDB:5G5H"
FT BINDING 468..470
FT /ligand="Mo-molybdopterin cytosine dinucleotide"
FT /ligand_id="ChEBI:CHEBI:71308"
FT /evidence="ECO:0000269|PubMed:27622978,
FT ECO:0007744|PDB:5G5G, ECO:0007744|PDB:5G5H"
FT BINDING 511..512
FT /ligand="Mo-molybdopterin cytosine dinucleotide"
FT /ligand_id="ChEBI:CHEBI:71308"
FT /evidence="ECO:0000269|PubMed:27622978,
FT ECO:0007744|PDB:5G5G, ECO:0007744|PDB:5G5H"
FT BINDING 615..621
FT /ligand="Mo-molybdopterin cytosine dinucleotide"
FT /ligand_id="ChEBI:CHEBI:71308"
FT /evidence="ECO:0000269|PubMed:27622978,
FT ECO:0007744|PDB:5G5G, ECO:0007744|PDB:5G5H"
FT BINDING 625
FT /ligand="Mo-molybdopterin cytosine dinucleotide"
FT /ligand_id="ChEBI:CHEBI:71308"
FT /evidence="ECO:0000269|PubMed:27622978,
FT ECO:0007744|PDB:5G5G, ECO:0007744|PDB:5G5H"
FT BINDING 688..691
FT /ligand="Mo-molybdopterin cytosine dinucleotide"
FT /ligand_id="ChEBI:CHEBI:71308"
FT /evidence="ECO:0000269|PubMed:27622978,
FT ECO:0007744|PDB:5G5G, ECO:0007744|PDB:5G5H"
FT MUTAGEN 440
FT /note="R->H,K: Decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:27622978"
FT MUTAGEN 692
FT /note="E->Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19368556"
FT HELIX 11..14
FT /evidence="ECO:0007829|PDB:5G5G"
FT HELIX 27..31
FT /evidence="ECO:0007829|PDB:5G5G"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:5G5G"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:5G5G"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:5G5G"
FT STRAND 57..67
FT /evidence="ECO:0007829|PDB:5G5G"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:5G5G"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:5G5G"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:5G5G"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:5G5G"
FT STRAND 111..119
FT /evidence="ECO:0007829|PDB:5G5G"
FT HELIX 120..127
FT /evidence="ECO:0007829|PDB:5G5G"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:5G5G"
FT HELIX 143..147
FT /evidence="ECO:0007829|PDB:5G5G"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:5G5G"
FT HELIX 165..171
FT /evidence="ECO:0007829|PDB:5G5G"
FT STRAND 173..182
FT /evidence="ECO:0007829|PDB:5G5G"
FT STRAND 194..200
FT /evidence="ECO:0007829|PDB:5G5G"
FT STRAND 203..208
FT /evidence="ECO:0007829|PDB:5G5G"
FT HELIX 213..224
FT /evidence="ECO:0007829|PDB:5G5G"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:5G5G"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:5G5G"
FT TURN 242..245
FT /evidence="ECO:0007829|PDB:5G5G"
FT HELIX 250..262
FT /evidence="ECO:0007829|PDB:5G5G"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:5G5G"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:5G5G"
FT HELIX 275..278
FT /evidence="ECO:0007829|PDB:5G5G"
FT STRAND 285..293
FT /evidence="ECO:0007829|PDB:5G5G"
FT STRAND 299..311
FT /evidence="ECO:0007829|PDB:5G5G"
FT HELIX 321..324
FT /evidence="ECO:0007829|PDB:5G5G"
FT STRAND 330..340
FT /evidence="ECO:0007829|PDB:5G5G"
FT HELIX 354..372
FT /evidence="ECO:0007829|PDB:5G5G"
FT HELIX 376..382
FT /evidence="ECO:0007829|PDB:5G5G"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:5G5G"
FT STRAND 391..397
FT /evidence="ECO:0007829|PDB:5G5G"
FT HELIX 401..412
FT /evidence="ECO:0007829|PDB:5G5G"
FT HELIX 414..416
FT /evidence="ECO:0007829|PDB:5G5G"
FT STRAND 429..441
FT /evidence="ECO:0007829|PDB:5G5G"
FT STRAND 447..453
FT /evidence="ECO:0007829|PDB:5G5G"
FT STRAND 459..462
FT /evidence="ECO:0007829|PDB:5G5G"
FT STRAND 468..470
FT /evidence="ECO:0007829|PDB:5G5G"
FT HELIX 472..484
FT /evidence="ECO:0007829|PDB:5G5G"
FT HELIX 488..490
FT /evidence="ECO:0007829|PDB:5G5G"
FT STRAND 491..494
FT /evidence="ECO:0007829|PDB:5G5G"
FT HELIX 511..534
FT /evidence="ECO:0007829|PDB:5G5G"
FT HELIX 538..540
FT /evidence="ECO:0007829|PDB:5G5G"
FT STRAND 541..544
FT /evidence="ECO:0007829|PDB:5G5G"
FT STRAND 547..550
FT /evidence="ECO:0007829|PDB:5G5G"
FT STRAND 553..556
FT /evidence="ECO:0007829|PDB:5G5G"
FT HELIX 557..560
FT /evidence="ECO:0007829|PDB:5G5G"
FT TURN 561..563
FT /evidence="ECO:0007829|PDB:5G5G"
FT STRAND 566..574
FT /evidence="ECO:0007829|PDB:5G5G"
FT HELIX 577..580
FT /evidence="ECO:0007829|PDB:5G5G"
FT STRAND 584..596
FT /evidence="ECO:0007829|PDB:5G5G"
FT TURN 597..599
FT /evidence="ECO:0007829|PDB:5G5G"
FT STRAND 602..612
FT /evidence="ECO:0007829|PDB:5G5G"
FT HELIX 619..638
FT /evidence="ECO:0007829|PDB:5G5G"
FT TURN 646..649
FT /evidence="ECO:0007829|PDB:5G5G"
FT STRAND 650..653
FT /evidence="ECO:0007829|PDB:5G5G"
FT TURN 656..658
FT /evidence="ECO:0007829|PDB:5G5G"
FT HELIX 664..666
FT /evidence="ECO:0007829|PDB:5G5G"
FT STRAND 669..674
FT /evidence="ECO:0007829|PDB:5G5G"
FT TURN 680..682
FT /evidence="ECO:0007829|PDB:5G5G"
FT HELIX 693..695
FT /evidence="ECO:0007829|PDB:5G5G"
FT HELIX 698..710
FT /evidence="ECO:0007829|PDB:5G5G"
FT STRAND 716..718
FT /evidence="ECO:0007829|PDB:5G5G"
FT HELIX 721..723
FT /evidence="ECO:0007829|PDB:5G5G"
FT HELIX 725..727
FT /evidence="ECO:0007829|PDB:5G5G"
SQ SEQUENCE 732 AA; 78088 MW; AF198715794F0138 CRC64;
MKFDKPAGEN PIDQLKVVGR PHDRIDGPLK TTGTARYAYE WHEEAPNAAY GYIVGSAIAK
GRLTALDTDA AQKAPGVLAV ITASNAGALG KGDKNTARLL GGPTIEHYHQ AIALVVAETF
EQARAAASLV QAHYRRNKGA YSLADEKQAV NQPPEDTPDK NVGDFDGAFT SAAVKIDATY
TTPDQSHMAM EPHASMAVWD GNKLTLWTSN QMIDWCRTDL AKTLKVPVEN VRIISPYIGG
GFGGKLFLRS DALLAALAAR AVKRPVKVML PRPSIPNNTT HRPATLQHLR IGADQSGKIT
AISHESWSGN LPGGTPETAV QQSELLYAGA NRHTGLRLAT LDLPEGNAMR APGEAPGLMA
LEIAIDELAE KAGIDPVEFR ILNDTQVDPA DPTRCFSRRQ LIECLRTGAD KFGWKQRNAT
PGQVRDGEWL VGHGVAAGFR NNLLEKSGAR VHLEQNGTVT VETDMTDIGT GSYTILAQTA
AEMLGVPLEQ VAVHLGDSSF PVSAGSGGQW GANTSTSGVY AACMKLREMI ASAVGFDPEQ
SQFADGKITN GTRSATLHEA TAGGRLTAEE SIEFGTLSKE YQQSTFAGHF VEVGVHSATG
EVRVRRMLAV CAAGRILNPK TARSQVIGAM TMGMGAALME ELAVDDRLGY FVNHDMAGYE
VPVHADIPKQ EVIFLDDTDP ISSPMKAKGV GELGLCGVSA AIANAVYNAT GIRVRDYPIT
LDKLLDKLPD VV
