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Acetophenone carboxylase beta subunit (EC 6.4.1.8) (Acetophenone carboxylase 15 kDa subunit)

 APCB_AROAE              Reviewed;         129 AA.
Q5P5G3;
05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
04-JAN-2005, sequence version 1.
30-AUG-2017, entry version 62.
RecName: Full=Acetophenone carboxylase beta subunit;
EC=6.4.1.8;
AltName: Full=Acetophenone carboxylase 15 kDa subunit;
Name=apc2; Synonyms=apcB; OrderedLocusNames=AZOSEA13240;
ORFNames=c1A200;
Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)).
Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
Rhodocyclaceae; Aromatoleum.
NCBI_TaxID=76114;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=EbN1;
PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
Reinhardt R.;
"The genome sequence of an anaerobic aromatic-degrading denitrifying
bacterium, strain EbN1.";
Arch. Microbiol. 183:27-36(2005).
[2]
IDENTIFICATION.
PubMed=12420173; DOI=10.1007/s00203-002-0487-2;
Rabus R., Kube M., Beck A., Widdel F., Reinhardt R.;
"Genes involved in the anaerobic degradation of ethylbenzene in a
denitrifying bacterium, strain EbN1.";
Arch. Microbiol. 178:506-516(2002).
[3]
FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL
PROPERTIES, COFACTOR, AND SUBUNIT.
PubMed=20047908; DOI=10.1128/JB.01423-09;
Jobst B., Schuhle K., Linne U., Heider J.;
"ATP-dependent carboxylation of acetophenone by a novel type of
carboxylase.";
J. Bacteriol. 192:1387-1394(2010).
-!- FUNCTION: Catalyzes the carboxylation of acetophenone to form 3-
oxo-3-phenylpropanoate (benzoylacetate) in the anaerobic
catabolism of ethylbenzene. Also carboxylates propiophenone at the
same rate and 4-acetyl-pyridine at lower rates.
{ECO:0000269|PubMed:20047908}.
-!- CATALYTIC ACTIVITY: 2 ATP + acetophenone + HCO(3)(-) + H(2)O +
H(+) = 2 ADP + 2 phosphate + 3-oxo-3-phenylpropanoate.
{ECO:0000269|PubMed:20047908}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:20047908};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:20047908};
Note=Divalent metal cations. Magnesium or manganese are required
for activity. {ECO:0000269|PubMed:20047908};
-!- ENZYME REGULATION: Inhibited by zinc ions, carbamoylphosphate and
beta,gamma-imido-ATP. {ECO:0000269|PubMed:20047908}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=33 uM for acetophone {ECO:0000269|PubMed:20047908};
KM=0.54 mM for HCO(3)(-) {ECO:0000269|PubMed:20047908};
KM=0.5 mM for ATP {ECO:0000269|PubMed:20047908};
Vmax=51 mmol/min/mg enzyme {ECO:0000269|PubMed:20047908};
Note=Kinetic parameters have been established using the
heteromeric complex including recombinant Apc5.;
-!- SUBUNIT: Acetophenone carboxylase consists of five subunits; a
heterooctameric subcomplex of two alpha (Apc1), two beta (Apc2),
two gamma (Apc3) and two delta (Apc4) subunits assembles with the
epsilon (Apc5) subunit in an unknown stoichiometry.
{ECO:0000269|PubMed:20047908}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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EMBL; CR555306; CAI07449.1; -; Genomic_DNA.
RefSeq; WP_011237169.1; NC_006513.1.
PDB; 5L9W; X-ray; 2.90 A; C=1-129.
PDBsum; 5L9W; -.
SMR; Q5P5G3; -.
STRING; 76114.c1A200; -.
EnsemblBacteria; CAI07449; CAI07449; c1A200.
KEGG; eba:c1A200; -.
eggNOG; ENOG4105RQI; Bacteria.
eggNOG; ENOG4111XDK; LUCA.
HOGENOM; HOG000224775; -.
KO; K10701; -.
OMA; GHPPLHD; -.
OrthoDB; POG091H11OK; -.
BioCyc; MetaCyc:MONOMER-14361; -.
Proteomes; UP000006552; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
InterPro; IPR016750; Aceto_COase_bsu/gsu.
Pfam; PF08882; Acetone_carb_G; 1.
PIRSF; PIRSF019217; Acetone_carboxlyase_gsu; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Complete proteome; Cytoplasm; Ligase;
Nucleotide-binding; Reference proteome.
CHAIN 1 129 Acetophenone carboxylase beta subunit.
/FTId=PRO_0000419042.
STRAND 8 14 {ECO:0000244|PDB:5L9W}.
TURN 15 18 {ECO:0000244|PDB:5L9W}.
STRAND 19 22 {ECO:0000244|PDB:5L9W}.
TURN 23 25 {ECO:0000244|PDB:5L9W}.
STRAND 28 31 {ECO:0000244|PDB:5L9W}.
HELIX 36 39 {ECO:0000244|PDB:5L9W}.
STRAND 40 45 {ECO:0000244|PDB:5L9W}.
HELIX 47 49 {ECO:0000244|PDB:5L9W}.
STRAND 57 59 {ECO:0000244|PDB:5L9W}.
TURN 65 67 {ECO:0000244|PDB:5L9W}.
STRAND 69 74 {ECO:0000244|PDB:5L9W}.
TURN 76 78 {ECO:0000244|PDB:5L9W}.
STRAND 81 87 {ECO:0000244|PDB:5L9W}.
STRAND 97 99 {ECO:0000244|PDB:5L9W}.
HELIX 101 110 {ECO:0000244|PDB:5L9W}.
STRAND 111 116 {ECO:0000244|PDB:5L9W}.
STRAND 119 121 {ECO:0000244|PDB:5L9W}.
SEQUENCE 129 AA; 14993 MW; 59C63ADA65DF13B0 CRC64;
MYERIRFTEY LDLDLNDEHW YCHDCGTKLI SARESYKKGC LVAERRPHEI HNPVIEGEYS
FAPDENWVRI LEFYCPGCTR QIETEYLPPG HPITVDIEVD IDSLKARLKK GVIVIKDGKL
TKPEAEVLA


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