APCD_AROAE
ID APCD_AROAE Reviewed; 684 AA.
AC Q5P5G5;
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 delta subunit;
DE EC=6.4.1.8;
DE AltName: Full=Acetophenone carboxylase 75 kDa subunit;
GN Name=apc4; Synonyms=apcD; OrderedLocusNames=AZOSEA13220; ORFNames=c1A100;
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 2-29, 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; CAI07447.1; -; Genomic_DNA.
DR RefSeq; WP_011237167.1; NC_006513.1.
DR PDB; 5L9W; X-ray; 2.90 A; A=1-684.
DR PDBsum; 5L9W; -.
DR AlphaFoldDB; Q5P5G5; -.
DR SMR; Q5P5G5; -.
DR STRING; 76114.c1A100; -.
DR EnsemblBacteria; CAI07447; CAI07447; c1A100.
DR KEGG; eba:c1A100; -.
DR eggNOG; COG0146; Bacteria.
DR HOGENOM; CLU_020413_2_0_4; -.
DR OMA; CGHGKYR; -.
DR OrthoDB; 1018930at2; -.
DR BioCyc; MetaCyc:MON-14363; -.
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; IPR003692; Hydantoinase_B.
DR InterPro; IPR045079; Oxoprolinase_fam.
DR PANTHER; PTHR11365; PTHR11365; 1.
DR Pfam; PF02538; Hydantoinase_B; 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..684
FT /note="Acetophenone carboxylase delta subunit"
FT /id="PRO_0000419041"
FT HELIX 6..13
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 20..27
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 31..53
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 92..102
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:5L9W"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 126..135
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 138..147
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 176..181
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 187..197
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 201..229
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 231..254
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 258..270
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 273..287
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 290..295
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 310..324
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 333..336
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 339..343
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 360..363
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 365..379
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 385..387
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 399..404
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 410..416
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 417..419
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 420..422
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 439..441
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 449..455
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 456..459
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 463..466
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 473..475
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 480..487
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 489..497
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 502..504
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 510..512
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 521..525
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 529..534
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 544..549
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 555..560
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 564..570
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 573..579
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 589..591
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 594..602
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 608..615
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 623..625
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 629..645
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 649..656
FT /evidence="ECO:0007829|PDB:5L9W"
FT HELIX 664..666
FT /evidence="ECO:0007829|PDB:5L9W"
FT STRAND 667..669
FT /evidence="ECO:0007829|PDB:5L9W"
FT TURN 672..674
FT /evidence="ECO:0007829|PDB:5L9W"
SQ SEQUENCE 684 AA; 75405 MW; E76CB4D97E85464E CRC64;
MAIPTLEQKL TWLKPAPASS RELDLAAQID PAQFEIGFQR TNDILDEGMD VFVRSCRCAM
GVAGDSLVAI MTADGDIVNG SCGTYLHAVI PPLIIKYILE TYGDEIRDGD LWFANDAVYG
GVHNPDQMVC MPVYYEGKLV AWTAALVHTT ETGAIEPGGM PVSATTRFEE GMNLPPMRIG
ENFKLREDVV SMFVAFGLRA PSMIAVDLKA RCTTADRVRT RIIELCEREG ADYVTGLFRK
MLQVAEAGAR ELIEQWPDGK YRCVTFSDAV GLKQGLVRSC YMTLEKKGDR MLVDLSETGP
ETPSPYNAHP QAAIAHFSNY IYEYLFHSLP ISNGTFANID FKFGKNTCLS PDPRAATSCS
VMISTGVMSA VHNACAKAMF STSLWKQSGA SMGNGGNALV LAGQNQWGSS FADMLAYSIN
TEGQGARPTE DGMDAFGFPW CVFGRAPNTE SVENEFPLLV PLSNHWKDSC GHGKYRGGVG
TAQVWVAHHV PELYMMAIAD NTKLQTPQPL FGGYAPCTVP GIGIRNANIK ELMAEGSDKI
KLDVETLLAE RTIDGKYEIE FQGRSVRPYS NGEVVTFAFS CGGTGYGDPL DRDPKSVEVD
LLKGVLTEQT AQNIYKVKWD ANLRRVDLDE TSRLRAAEHD ARRKRGVPYE QFEREWLKQR
PDDEILKYYG TWPDAKVAQP LLRA
