APCC_AROAE
ID APCC_AROAE Reviewed; 732 AA.
AC Q5P5G4;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Acetophenone carboxylase gamma subunit;
DE EC=6.4.1.8;
DE AltName: Full=Acetophenone carboxylase 87 kDa subunit;
GN Name=apc3; Synonyms=apcC; OrderedLocusNames=AZOSEA13230; ORFNames=c1A102;
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 PROTEIN SEQUENCE OF 2-36, AND INDUCTION.
RX PubMed=10941798;
RA Champion K.M., Zengler K., Rabus R.;
RT "Anaerobic degradation of ethylbenzene and toluene in denitrifying strain
RT EbN1 proceeds via independent substrate-induced pathways.";
RL J. Mol. Microbiol. Biotechnol. 1:157-164(1999).
RN [3]
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 [4]
RP INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15687214; DOI=10.1128/jb.187.4.1493-1503.2005;
RA Kuhner S., Wohlbrand L., Fritz I., Wruck W., Hultschig C., Hufnagel P.,
RA Kube M., Reinhardt R., Rabus R.;
RT "Substrate-dependent regulation of anaerobic degradation pathways for
RT toluene and ethylbenzene in a denitrifying bacterium, strain EbN1.";
RL J. Bacteriol. 187:1493-1503(2005).
RN [5]
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}.
CC -!- INDUCTION: By ethylbenzene, toluene and acetophenone.
CC {ECO:0000269|PubMed:10941798, ECO:0000269|PubMed:15687214}.
CC -!- SIMILARITY: Belongs to the HyuA family. {ECO:0000305}.
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DR EMBL; CR555306; CAI07448.1; -; Genomic_DNA.
DR RefSeq; WP_011237168.1; NC_006513.1.
DR PDB; 5L9W; X-ray; 2.90 A; B=1-732.
DR PDBsum; 5L9W; -.
DR AlphaFoldDB; Q5P5G4; -.
DR SMR; Q5P5G4; -.
DR STRING; 76114.c1A102; -.
DR EnsemblBacteria; CAI07448; CAI07448; c1A102.
DR KEGG; eba:c1A102; -.
DR eggNOG; COG0145; Bacteria.
DR HOGENOM; CLU_002157_1_2_4; -.
DR OMA; QPVRYFQ; -.
DR OrthoDB; 327092at2; -.
DR BioCyc; MetaCyc:MON-14362; -.
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:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR InterPro; IPR008040; Hydant_A_N.
DR InterPro; IPR002821; Hydantoinase_A.
DR InterPro; IPR045079; Oxoprolinase_fam.
DR PANTHER; PTHR11365; PTHR11365; 1.
DR Pfam; PF05378; Hydant_A_N; 1.
DR Pfam; PF01968; Hydantoinase_A; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Direct protein sequencing; Ligase;
KW Nucleotide-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10941798"
FT CHAIN 2..732
FT /note="Acetophenone carboxylase gamma subunit"
FT /id="PRO_0000419040"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 19..28
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 31..38
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 44..57
FT /evidence="ECO:0007829|PDB:5L9W"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 79..85
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:5L9W"
FT TURN 107..110
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 118..121
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 158..170
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:5L9W"
FT TURN 181..185
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 188..200
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 214..217
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 223..253
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 258..263
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:5L9W"
FT TURN 280..282
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 283..298
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 304..309
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 314..319
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 327..330
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 346..349
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 354..358
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 365..371
FT /evidence="ECO:0007829|PDB:5L9W"
FT TURN 373..376
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 379..381
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 390..396
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 414..424
FT /evidence="ECO:0007829|PDB:5L9W"
FT TURN 425..430
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 433..458
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 463..465
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 467..474
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 475..482
FT /evidence="ECO:0007829|PDB:5L9W"
FT TURN 483..485
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 487..491
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 495..505
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 508..521
FT /evidence="ECO:0007829|PDB:5L9W"
FT TURN 523..525
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 532..552
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 557..559
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 561..570
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 577..580
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 589..606
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 609..611
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 614..616
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 618..629
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 647..649
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 650..658
FT /evidence="ECO:0007829|PDB:5L9W"
FT TURN 659..662
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 663..671
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 672..674
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 683..688
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 693..696
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 700..704
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 710..716
FT /evidence="ECO:0007829|PDB:5L9W"
SQ SEQUENCE 732 AA; 80339 MW; FBFF7C5053578155 CRC64;
MSSLTNQDAI NSIDIDVGGT FTDFVLTLDG ERHIAKCPTT PHDLSIGFLN AVEAGGDKVG
LSVEELLPRI DIIRYSTTVA LNRLLQRQGP RIGLLTTEGH EDAILIGRGA QWTDGQRVAE
RRNIAVQNKP LPLIERDLIL GVRERIDSSG SVVRPLDEED VRTKLRMLMD RGARAIVVSL
LWSFMNPAHE KRVREIIREE YKEYHIGFVP VVMSHSVVSK IGEYERTMTA VLDAYLQRSM
QNDIGATWDK LRAKGYHGAF LMIHNSGGSA DIFKTPASRT FNGGPVAGLM GSAYFANKLG
YKNVVAGDVG GTSFDVALVV ESSVRNYTFR PVIDKWMVNV TMMQTISVGS GGGSIAKVDR
SGTRLEVGPR SAGSMPGPVC YDLGGTEPTV TDADVVLGYI NPDTYYGGRM PLNKAKAEKA
IREKIAQPLG IETIEAAALI RYIVDENMAS AIKREVHMRG YHPEDFVLFA FGGAGPTHMA
GLKGDIPKAV VFPAAPVFCA MGSSIMDIVH MYEQSRRMVF MEPGTEKFVV DYEHFNQTVD
TMIERARQEL RSEGLEVDDA SFGLELDMLY GGQVNLKRMS SPLLHIRTAE DALKVYQAFE
TEFSEAFSPL VVNKPGGVFL DNFVLRVTVP TWKPPIPEYP LQGTDPSAAF LGKRKAYWPE
TKHWADTPTY QFELLQAGNV IDGPAIVEAE LTTIVVPPRQ RLSIDTHGLA ILEAIDPAPP
TKRVSAAAAA IV
