APCA_AROAE
ID APCA_AROAE Reviewed; 658 AA.
AC Q5P5G2;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Acetophenone carboxylase alpha subunit;
DE EC=6.4.1.8;
DE AltName: Full=Acetophenone carboxylase 70 kDa subunit;
GN Name=apc1; Synonyms=apcA; OrderedLocusNames=AZOSEA13250; ORFNames=c1A105;
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 1-31, 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 oxoprolinase family. {ECO:0000305}.
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DR EMBL; CR555306; CAI07450.1; -; Genomic_DNA.
DR RefSeq; WP_011237170.1; NC_006513.1.
DR PDB; 5L9W; X-ray; 2.90 A; b=1-658.
DR PDBsum; 5L9W; -.
DR AlphaFoldDB; Q5P5G2; -.
DR SMR; Q5P5G2; -.
DR STRING; 76114.c1A105; -.
DR EnsemblBacteria; CAI07450; CAI07450; c1A105.
DR KEGG; eba:c1A105; -.
DR eggNOG; COG0145; Bacteria.
DR HOGENOM; CLU_002157_1_2_4; -.
DR OMA; RTPMIEI; -.
DR OrthoDB; 327092at2; -.
DR BioCyc; MetaCyc:MON-14360; -.
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 CHAIN 1..658
FT /note="Acetophenone carboxylase alpha subunit"
FT /id="PRO_0000419039"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 10..18
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 35..49
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 55..60
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 62..69
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 71..77
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:5L9W"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 123..135
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 153..165
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 179..182
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 188..220
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 243..246
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 249..264
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 270..274
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 280..286
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 292..298
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 301..308
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 336..339
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 341..343
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 353..359
FT /evidence="ECO:0007829|PDB:5L9W"
FT TURN 365..369
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 377..387
FT /evidence="ECO:0007829|PDB:5L9W"
FT TURN 388..393
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 396..422
FT /evidence="ECO:0007829|PDB:5L9W"
FT TURN 426..428
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 430..435
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 438..449
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 454..456
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 460..462
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 463..469
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 473..478
FT /evidence="ECO:0007829|PDB:5L9W"
FT TURN 490..492
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 493..510
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 515..517
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 518..524
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 538..542
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 547..559
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 569..575
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 601..603
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 614..616
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 622..630
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 635..638
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 643..646
FT /evidence="ECO:0007829|PDB:5L9W"
SQ SEQUENCE 658 AA; 69867 MW; 867F0B8A90A1FB89 CRC64;
MYTVDIDTGG TMTDALVSDG EQRHAIKVDT TPHDYTVSFN GCLSEAAKRL GYPSTEAFLA
KVGMIRWSST ITTNVLGERR GSKVGLLVTE GNEENLYGTV QSPVVGELVD ERNIIGLPSN
PTAVDILSGV KQLLEGGVRR ICVCLANAFP DNGAEREIKA VIEDQYPDHI IGAVPVLLGS
EMAPLRHDQT RVHYSLMNAY THTQLATSLF KAEDLLRDDH NWTGPLLIGN TNGGVARIGK
TKSVDTIESG PVFGTFGGAY MARLYGLKDV VCFDVGGTTT KASIIRDGQP MFQRGGELME
VPVQSSFAML RSAVVGGGSI ARVRDKSVTL GPESMGAAPG PACYGLGGNE ATLTDALLAL
GYLDPNNFLG GRRQLKVDLA RAAIERNVAK PLGVSLEVAA LSIRDEAVAM MTELLQATLA
EAKLTAQDAA LFAFGGNGPM FAAFVAERLG VQAAYAFNLG PVFSAFGSAI SDVVHVYERG
VDLRWNATVK GQLLPTLDAL QTQAERDLKG ESFDPAKAAY VWELDFGTTE AEVSTVRAEL
AQSAASTVLD ALTQAVTAAG VASLPLLGAR LSSRFVVGAH GMKKRADRVP AEAPASREMR
FNGASEAASP VYRWETMNVG DIAVGPAVVN GSTLTCPIPP RWQLRVDDYG NAELSRAQ
