APCB_AROAE
ID APCB_AROAE Reviewed; 129 AA.
AC Q5P5G3;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Acetophenone carboxylase beta subunit;
DE EC=6.4.1.8;
DE AltName: Full=Acetophenone carboxylase 15 kDa subunit;
GN Name=apc2; Synonyms=apcB; OrderedLocusNames=AZOSEA13240; ORFNames=c1A200;
OS Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Aromatoleum.
OX NCBI_TaxID=76114;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EbN1;
RX PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA Reinhardt R.;
RT "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT bacterium, strain EbN1.";
RL Arch. Microbiol. 183:27-36(2005).
RN [2]
RP IDENTIFICATION.
RX PubMed=12420173; DOI=10.1007/s00203-002-0487-2;
RA Rabus R., Kube M., Beck A., Widdel F., Reinhardt R.;
RT "Genes involved in the anaerobic degradation of ethylbenzene in a
RT denitrifying bacterium, strain EbN1.";
RL Arch. Microbiol. 178:506-516(2002).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, COFACTOR, AND SUBUNIT.
RX PubMed=20047908; DOI=10.1128/jb.01423-09;
RA Jobst B., Schuhle K., Linne U., Heider J.;
RT "ATP-dependent carboxylation of acetophenone by a novel type of
RT carboxylase.";
RL J. Bacteriol. 192:1387-1394(2010).
CC -!- FUNCTION: Catalyzes the carboxylation of acetophenone to form 3-oxo-3-
CC phenylpropanoate (benzoylacetate) in the anaerobic catabolism of
CC ethylbenzene. Also carboxylates propiophenone at the same rate and 4-
CC acetyl-pyridine at lower rates. {ECO:0000269|PubMed:20047908}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetophenone + 2 ATP + H2O + hydrogencarbonate = 3-oxo-3-
CC phenylpropanoate + 2 ADP + 2 H(+) + 2 phosphate;
CC Xref=Rhea:RHEA:28647, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:22731, ChEBI:CHEBI:27632,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=6.4.1.8;
CC Evidence={ECO:0000269|PubMed:20047908};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:20047908};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:20047908};
CC Note=Divalent metal cations. Magnesium or manganese are required for
CC activity. {ECO:0000269|PubMed:20047908};
CC -!- ACTIVITY REGULATION: Inhibited by zinc ions, carbamoylphosphate and
CC beta,gamma-imido-ATP. {ECO:0000269|PubMed:20047908}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=33 uM for acetophone {ECO:0000269|PubMed:20047908};
CC KM=0.54 mM for HCO(3)(-) {ECO:0000269|PubMed:20047908};
CC KM=0.5 mM for ATP {ECO:0000269|PubMed:20047908};
CC Vmax=51 mmol/min/mg enzyme {ECO:0000269|PubMed:20047908};
CC Note=Kinetic parameters have been established using the heteromeric
CC complex including recombinant Apc5.;
CC -!- SUBUNIT: Acetophenone carboxylase consists of five subunits; a
CC heterooctameric subcomplex of two alpha (Apc1), two beta (Apc2), two
CC gamma (Apc3) and two delta (Apc4) subunits assembles with the epsilon
CC (Apc5) subunit in an unknown stoichiometry.
CC {ECO:0000269|PubMed:20047908}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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DR EMBL; CR555306; CAI07449.1; -; Genomic_DNA.
DR RefSeq; WP_011237169.1; NC_006513.1.
DR PDB; 5L9W; X-ray; 2.90 A; C=1-129.
DR PDBsum; 5L9W; -.
DR AlphaFoldDB; Q5P5G3; -.
DR SMR; Q5P5G3; -.
DR STRING; 76114.c1A200; -.
DR PRIDE; Q5P5G3; -.
DR EnsemblBacteria; CAI07449; CAI07449; c1A200.
DR KEGG; eba:c1A200; -.
DR eggNOG; COG4647; Bacteria.
DR HOGENOM; CLU_153790_0_0_4; -.
DR OMA; GHPPLHD; -.
DR OrthoDB; 1828138at2; -.
DR BioCyc; MetaCyc:MON-14361; -.
DR BRENDA; 6.4.1.8; 12182.
DR Proteomes; UP000006552; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR InterPro; IPR016750; Aceto_COase_bsu/gsu.
DR Pfam; PF08882; Acetone_carb_G; 1.
DR PIRSF; PIRSF019217; Acetone_carboxlyase_gsu; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Ligase; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..129
FT /note="Acetophenone carboxylase beta subunit"
FT /id="PRO_0000419042"
FT STRAND 8..14
FT /evidence="ECO:0007829|PDB:5L9W"
FT TURN 15..18
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 19..22
FT /evidence="ECO:0007829|PDB:5L9W"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 36..39
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:5L9W"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:5L9W"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 101..110
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:5L9W"
SQ SEQUENCE 129 AA; 14993 MW; 59C63ADA65DF13B0 CRC64;
MYERIRFTEY LDLDLNDEHW YCHDCGTKLI SARESYKKGC LVAERRPHEI HNPVIEGEYS
FAPDENWVRI LEFYCPGCTR QIETEYLPPG HPITVDIEVD IDSLKARLKK GVIVIKDGKL
TKPEAEVLA
