PANZ_ECOLI
ID PANZ_ECOLI Reviewed; 127 AA.
AC P37613; Q2M7C2;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=PanD regulatory factor {ECO:0000255|HAMAP-Rule:MF_02018, ECO:0000305};
GN Name=panZ {ECO:0000255|HAMAP-Rule:MF_02018, ECO:0000303|PubMed:23170229};
GN Synonyms=panM {ECO:0000250|UniProtKB:Q7CPJ9}, yhhK;
GN OrderedLocusNames=b3459, JW3424;
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;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
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 INTERACTION WITH PAND, AND SUBUNIT.
RX PubMed=22940551; DOI=10.1016/j.bbrc.2012.08.084;
RA Monteiro D.C., Rugen M.D., Shepherd D., Nozaki S., Niki H., Webb M.E.;
RT "Formation of a heterooctameric complex between aspartate alpha-
RT decarboxylase and its cognate activating factor, PanZ, is CoA-dependent.";
RL Biochem. Biophys. Res. Commun. 426:350-355(2012).
RN [5]
RP FUNCTION, INTERACTION WITH PAND, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=23170229; DOI=10.1002/mbo3.34;
RA Nozaki S., Webb M.E., Niki H.;
RT "An activator for pyruvoyl-dependent l-aspartate alpha-decarboxylase is
RT conserved in a small group of the gamma-proteobacteria including
RT Escherichia coli.";
RL MicrobiologyOpen 1:298-310(2012).
RN [6] {ECO:0007744|PDB:2K5T}
RP STRUCTURE BY NMR IN COMPLEX WITH COENZYME A.
RA Cort J.R., Yee A., Arrowsmith C.H., Kennedy M.A.;
RT "Solution NMR structure of putative N-acetyl transferase YhhK from E. coli
RT bound to coenzyme A.";
RL Submitted (JUN-2008) to the PDB data bank.
RN [7] {ECO:0007744|PDB:4CRY}
RP X-RAY CRYSTALLOGRAPHY (1.61 ANGSTROMS) IN COMPLEX WITH PAND AND ACETYL
RP COENZYME A.
RA Monteiro D.C.F., Patel V., Bartlett C.P., Grant T.D., Nozaki S.,
RA Gowdy J.A., Snell E.H., Niki H., Pearson A.R., Webb M.E.;
RT "Direct visualisation of strain-induced protein post-translational
RT modification.";
RL Submitted (MAR-2014) to the PDB data bank.
RN [8] {ECO:0007744|PDB:4CRZ, ECO:0007744|PDB:4CS0}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEXES WITH PAND AND ACETYL
RP COENZYME A, FUNCTION, ACTIVITY REGULATION, INTERACTION WITH PAND, SUBUNIT,
RP AND MUTAGENESIS OF ASN-45.
RX PubMed=25910242; DOI=10.1016/j.chembiol.2015.03.017;
RA Monteiro D.C., Patel V., Bartlett C.P., Nozaki S., Grant T.D., Gowdy J.A.,
RA Thompson G.S., Kalverda A.P., Snell E.H., Niki H., Pearson A.R., Webb M.E.;
RT "The structure of the PanD/PanZ protein complex reveals negative feedback
RT regulation of pantothenate biosynthesis by coenzyme A.";
RL Chem. Biol. 22:492-503(2015).
CC -!- FUNCTION: Controls both the activation and catalytic activity of PanD
CC in a coenzyme A (CoA)-dependent fashion. Binding of CoA or a derivative
CC to PanZ leads to interaction with PanD, which promotes the processing
CC and activation of pro-PanD, and subsequent substrate-mediated
CC inhibition of the active form of PanD (PubMed:23170229,
CC PubMed:25910242). Inhibition of PanD activity is probably the primary
CC metabolic role of PanZ, allowing negative feedback regulation of
CC pantothenate biosynthesis by CoA (PubMed:25910242).
CC {ECO:0000269|PubMed:23170229, ECO:0000269|PubMed:25910242}.
CC -!- ACTIVITY REGULATION: Activation of PanD processing occurs even at low
CC CoA concentrations. In contrast, full inhibition of PanD catalytic
CC activity only occurs at sufficiently high CoA concentrations.
CC {ECO:0000269|PubMed:25910242}.
CC -!- SUBUNIT: Interacts with PanD in the presence of CoA (PubMed:23170229,
CC PubMed:22940551, PubMed:25910242). Forms a heterooctameric complex
CC composed of four PanD subunits and four PanZ subunits (PubMed:22940551,
CC PubMed:25910242). Monomer in solution (PubMed:22940551).
CC {ECO:0000269|PubMed:22940551, ECO:0000269|PubMed:23170229,
CC ECO:0000269|PubMed:25910242}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutants are deficient in the
CC biosynthetic pathway for pantothenate. {ECO:0000269|PubMed:23170229}.
CC -!- SIMILARITY: Belongs to the PanZ/PanM family. {ECO:0000255|HAMAP-
CC Rule:MF_02018, ECO:0000305}.
CC -!- CAUTION: Lacks the conserved catalytic glutamate found in many
CC enzymatically active members of the Gcn5-like N-acetyltransferase
CC (GNAT) family. {ECO:0000250|UniProtKB:Q7CPJ9}.
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DR EMBL; U00039; AAB18434.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76484.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77834.1; -; Genomic_DNA.
DR PIR; S47678; S47678.
DR RefSeq; NP_417916.1; NC_000913.3.
DR RefSeq; WP_000778768.1; NZ_SSZK01000008.1.
DR PDB; 2K5T; NMR; -; A=1-127.
DR PDB; 4CRY; X-ray; 1.61 A; B=1-127.
DR PDB; 4CRZ; X-ray; 1.70 A; B=1-127.
DR PDB; 4CS0; X-ray; 2.10 A; B=1-127.
DR PDB; 5LS7; X-ray; 1.16 A; B=1-127.
DR PDBsum; 2K5T; -.
DR PDBsum; 4CRY; -.
DR PDBsum; 4CRZ; -.
DR PDBsum; 4CS0; -.
DR PDBsum; 5LS7; -.
DR AlphaFoldDB; P37613; -.
DR BMRB; P37613; -.
DR SMR; P37613; -.
DR BioGRID; 4262496; 7.
DR IntAct; P37613; 2.
DR STRING; 511145.b3459; -.
DR jPOST; P37613; -.
DR PaxDb; P37613; -.
DR PRIDE; P37613; -.
DR DNASU; 947963; -.
DR EnsemblBacteria; AAC76484; AAC76484; b3459.
DR EnsemblBacteria; BAE77834; BAE77834; BAE77834.
DR GeneID; 947963; -.
DR KEGG; ecj:JW3424; -.
DR KEGG; eco:b3459; -.
DR PATRIC; fig|1411691.4.peg.3266; -.
DR EchoBASE; EB2125; -.
DR eggNOG; COG0456; Bacteria.
DR HOGENOM; CLU_135649_0_0_6; -.
DR InParanoid; P37613; -.
DR OMA; HFSDQDR; -.
DR PhylomeDB; P37613; -.
DR BioCyc; EcoCyc:EG12211-MON; -.
DR BioCyc; MetaCyc:EG12211-MON; -.
DR EvolutionaryTrace; P37613; -.
DR PRO; PR:P37613; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1905502; F:acetyl-CoA binding; IDA:EcoCyc.
DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR GO; GO:0043086; P:negative regulation of catalytic activity; IDA:EcoCyc.
DR GO; GO:0015940; P:pantothenate biosynthetic process; IMP:EcoCyc.
DR GO; GO:0031638; P:zymogen activation; IDA:EcoCyc.
DR HAMAP; MF_02018; PanZ_PanM; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR032900; PanZ.
DR InterPro; IPR040448; PanZ_GNAT.
DR Pfam; PF12568; PanZ; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Pantothenate biosynthesis; Reference proteome.
FT CHAIN 1..127
FT /note="PanD regulatory factor"
FT /id="PRO_0000169553"
FT DOMAIN 1..127
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02018"
FT REGION 43..48
FT /note="Interaction with PanD"
FT /evidence="ECO:0000269|PubMed:25910242"
FT REGION 66..76
FT /note="Interaction with PanD"
FT /evidence="ECO:0000269|PubMed:25910242"
FT BINDING 66..68
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02018,
FT ECO:0000269|PubMed:25910242, ECO:0000269|Ref.6,
FT ECO:0000269|Ref.7, ECO:0007744|PDB:2K5T"
FT BINDING 72..79
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02018,
FT ECO:0000269|PubMed:25910242, ECO:0000269|Ref.6,
FT ECO:0000269|Ref.7, ECO:0007744|PDB:2K5T"
FT MUTAGEN 45
FT /note="N->A: Loss of affinity for PanD. Is still able to
FT activate but not regulate the PanD protein."
FT /evidence="ECO:0000269|PubMed:25910242"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:5LS7"
FT HELIX 13..22
FT /evidence="ECO:0007829|PDB:5LS7"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:5LS7"
FT STRAND 37..44
FT /evidence="ECO:0007829|PDB:5LS7"
FT STRAND 47..57
FT /evidence="ECO:0007829|PDB:5LS7"
FT STRAND 60..68
FT /evidence="ECO:0007829|PDB:5LS7"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:5LS7"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:5LS7"
FT HELIX 77..88
FT /evidence="ECO:0007829|PDB:5LS7"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:5LS7"
FT HELIX 105..114
FT /evidence="ECO:0007829|PDB:5LS7"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:5LS7"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:5LS7"
SQ SEQUENCE 127 AA; 14506 MW; EF054A30D294519A CRC64;
MKLTIIRLEK FSDQDRIDLQ KIWPEYSPSS LQVDDNHRIY AARFNERLLA AVRVTLSGTE
GALDSLRVRE VTRRRGVGQY LLEEVLRNNP GVSCWWMADA GVEDRGVMTA FMQALGFTAQ
QGGWEKC
