SCACT_ACEAC
ID SCACT_ACEAC Reviewed; 505 AA.
AC B3EY95; M4MDU8; Q43882;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Succinyl-CoA:acetate CoA-transferase;
DE EC=2.8.3.18 {ECO:0000269|PubMed:18502856, ECO:0000269|PubMed:23030530, ECO:0000269|Ref.3};
DE AltName: Full=Succinyl-coenzyme A (CoA):acetate CoA-transferase {ECO:0000303|PubMed:18502856, ECO:0000303|PubMed:23030530};
DE Short=SCACT {ECO:0000303|PubMed:18502856};
OS Acetobacter aceti.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acetobacter; Acetobacter subgen. Acetobacter.
OX NCBI_TaxID=435 {ECO:0000312|EMBL:ACD85596.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, DISRUPTION PHENOTYPE,
RP AND FUNCTION.
RC STRAIN=1023 {ECO:0000312|EMBL:BAA02549.1};
RA Fukaya M., Takemura H., Tayama K., Okumura H., Kawamura Y., Horinouchi S.,
RA Beppu T.;
RT "The aarC gene responsible for acetic acid assimilation confers acetic acid
RT resistance on Acetobacter aceti.";
RL J. Ferment. Bioeng. 76:270-275(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT,
RP PATHWAY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=1023 {ECO:0000303|PubMed:18502856};
RX PubMed=18502856; DOI=10.1128/jb.00405-08;
RA Mullins E.A., Francois J.A., Kappock T.J.;
RT "A specialized citric acid cycle requiring succinyl-coenzyme A
RT (CoA):acetate CoA-transferase (AarC) confers acetic acid resistance on the
RT acidophile Acetobacter aceti.";
RL J. Bacteriol. 190:4933-4940(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP MUTAGENESIS OF CYS-357, PATHWAY, AND INDUCTION.
RC STRAIN=1023 {ECO:0000303|Ref.3};
RX DOI=10.4081/aab.2013.s1.e3;
RA Mullins E.A., Kappock T.J.;
RT "Functional analysis of the acetic acid resistance (aar) gene cluster in
RT Acetobacter aceti strain 1023.";
RL Acetic Acid Bacteria 2:E3-E3(2013).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) IN COMPLEXES WITH COENZYME A AND
RP ACETATE, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, AND
RP MUTAGENESIS OF GLU-435.
RX PubMed=23030530; DOI=10.1021/bi300957f;
RA Mullins E.A., Kappock T.J.;
RT "Crystal structures of Acetobacter aceti succinyl-coenzyme A (CoA):acetate
RT CoA-transferase reveal specificity determinants and illustrate the
RT mechanism used by class I CoA-transferases.";
RL Biochemistry 51:8422-8434(2012).
CC -!- FUNCTION: Utilizes succinyl-CoA to convert toxic acetate to acetyl-CoA
CC and succinate. Required for growth on acetic acid and for resistance to
CC high levels of acetic acid. Has also low activity with acetoacetate as
CC substrate. {ECO:0000269|PubMed:18502856, ECO:0000269|PubMed:23030530,
CC ECO:0000269|Ref.1, ECO:0000269|Ref.3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetate + succinyl-CoA = acetyl-CoA + succinate;
CC Xref=Rhea:RHEA:35711, ChEBI:CHEBI:30031, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57292; EC=2.8.3.18;
CC Evidence={ECO:0000269|PubMed:18502856, ECO:0000269|PubMed:23030530,
CC ECO:0000269|Ref.3};
CC -!- ACTIVITY REGULATION: Subject to competitive inhibition by coenzyme A
CC (CoA). {ECO:0000269|PubMed:18502856}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=70 mM for acetate {ECO:0000269|PubMed:18502856};
CC KM=22.1 mM for succinyl-CoA {ECO:0000269|PubMed:18502856};
CC KM=22.3 mM for acetyl-CoA {ECO:0000269|PubMed:18502856};
CC KM=0.9 mM for succinate {ECO:0000269|PubMed:18502856};
CC KM=130 mM for acetoacetate {ECO:0000269|PubMed:18502856};
CC Note=kcat is 280 sec(-1) with acetate. kcat is 201 sec(-1) with
CC succinyl-CoA. kcat is 75 sec(-1) with acetyl-CoA. kcat is 36.5 sec(-
CC 1) with acetoacetate. kcat is 70.9 sec(-1) with succinate.
CC {ECO:0000269|PubMed:18502856};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis.
CC {ECO:0000269|PubMed:18502856, ECO:0000269|Ref.3}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18502856,
CC ECO:0000269|PubMed:23030530}.
CC -!- INDUCTION: Expressed at intermediate levels during the first growth
CC phase, when ethanol is metabolized and acetic acid accumulates in the
CC growth medium. Up-regulated during the second growth phase, when
CC acetate is catabolized. {ECO:0000269|Ref.3}.
CC -!- DISRUPTION PHENOTYPE: Cells cannot grow on acetate and have lost the
CC resistance to high levels of acetate, a characteristic of wild-type
CC A.aceti. {ECO:0000269|Ref.1}.
CC -!- SIMILARITY: Belongs to the acetyl-CoA hydrolase/transferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA02549.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D13291; BAA02549.1; ALT_FRAME; Genomic_DNA.
DR EMBL; DQ631551; ACD85596.1; -; Genomic_DNA.
DR EMBL; JX475924; AGG68319.1; -; Genomic_DNA.
DR EMBL; JX475925; AGG68324.1; -; Genomic_DNA.
DR PIR; I39486; I39486.
DR PDB; 4EU3; X-ray; 1.58 A; A/B=1-505.
DR PDB; 4EU4; X-ray; 2.80 A; A/B=1-505.
DR PDB; 4EU5; X-ray; 1.74 A; A/B=1-505.
DR PDB; 4EU6; X-ray; 1.99 A; A/B=1-505.
DR PDB; 4EU7; X-ray; 1.70 A; A/B=1-505.
DR PDB; 4EU8; X-ray; 1.81 A; A/B=1-505.
DR PDB; 4EU9; X-ray; 1.48 A; A/B=1-505.
DR PDB; 4EUA; X-ray; 2.40 A; A/B=1-505.
DR PDB; 4EUB; X-ray; 1.97 A; A/B=1-505.
DR PDB; 4EUC; X-ray; 2.64 A; A/B=1-505.
DR PDB; 4EUD; X-ray; 1.95 A; A/B=1-505.
DR PDB; 5DDK; X-ray; 2.13 A; A/B=1-505.
DR PDB; 5DW4; X-ray; 1.62 A; A/B=1-505.
DR PDB; 5DW5; X-ray; 1.66 A; A/B=1-505.
DR PDB; 5DW6; X-ray; 1.55 A; A/B=1-505.
DR PDB; 5E5H; X-ray; 2.05 A; A/B=1-505.
DR PDBsum; 4EU3; -.
DR PDBsum; 4EU4; -.
DR PDBsum; 4EU5; -.
DR PDBsum; 4EU6; -.
DR PDBsum; 4EU7; -.
DR PDBsum; 4EU8; -.
DR PDBsum; 4EU9; -.
DR PDBsum; 4EUA; -.
DR PDBsum; 4EUB; -.
DR PDBsum; 4EUC; -.
DR PDBsum; 4EUD; -.
DR PDBsum; 5DDK; -.
DR PDBsum; 5DW4; -.
DR PDBsum; 5DW5; -.
DR PDBsum; 5DW6; -.
DR PDBsum; 5E5H; -.
DR AlphaFoldDB; B3EY95; -.
DR SMR; B3EY95; -.
DR KEGG; ag:ACD85596; -.
DR BioCyc; MetaCyc:MON-17982; -.
DR BRENDA; 2.8.3.18; 33.
DR BRENDA; 2.8.3.8; 33.
DR BRENDA; 6.2.1.5; 33.
DR SABIO-RK; B3EY95; -.
DR UniPathway; UPA00340; -.
DR GO; GO:0008775; F:acetate CoA-transferase activity; IEA:InterPro.
DR GO; GO:0003986; F:acetyl-CoA hydrolase activity; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IDA:UniProtKB.
DR GO; GO:0045733; P:acetate catabolic process; IDA:UniProtKB.
DR GO; GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IDA:UniProtKB.
DR GO; GO:0019679; P:propionate metabolic process, methylcitrate cycle; IEA:InterPro.
DR GO; GO:1901289; P:succinyl-CoA catabolic process; IDA:UniProtKB.
DR Gene3D; 3.40.1080.20; -; 1.
DR InterPro; IPR026888; AcetylCoA_hyd_C.
DR InterPro; IPR038460; AcetylCoA_hyd_C_sf.
DR InterPro; IPR003702; ActCoA_hydro.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR InterPro; IPR017821; Succinate_CoA_transferase.
DR Pfam; PF13336; AcetylCoA_hyd_C; 1.
DR Pfam; PF02550; AcetylCoA_hydro; 1.
DR SUPFAM; SSF100950; SSF100950; 2.
DR TIGRFAMs; TIGR03458; YgfH_subfam; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Transferase.
FT CHAIN 1..505
FT /note="Succinyl-CoA:acetate CoA-transferase"
FT /id="PRO_0000430783"
FT ACT_SITE 294
FT /note="5-glutamyl coenzyme A thioester intermediate"
FT /evidence="ECO:0000269|PubMed:23030530"
FT BINDING 269..273
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:23030530"
FT BINDING 364
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:23030530"
FT BINDING 384
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:23030530"
FT BINDING 388
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:23030530"
FT BINDING 408
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:23030530"
FT MUTAGEN 294
FT /note="E->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:23030530"
FT MUTAGEN 357
FT /note="C->Y: Strongly impaired protein solubility."
FT /evidence="ECO:0000269|Ref.3"
FT MUTAGEN 435
FT /note="E->A,Q: Abolishes protein solubility."
FT /evidence="ECO:0000269|PubMed:23030530"
FT CONFLICT 357
FT /note="C -> Y (in Ref. 3; AGG68324)"
FT HELIX 9..13
FT /evidence="ECO:0007829|PDB:4EU9"
FT HELIX 17..21
FT /evidence="ECO:0007829|PDB:4EU9"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:4EU9"
FT HELIX 43..57
FT /evidence="ECO:0007829|PDB:4EU9"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:4EU9"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:4EU9"
FT HELIX 77..82
FT /evidence="ECO:0007829|PDB:4EU9"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:4EU9"
FT HELIX 96..103
FT /evidence="ECO:0007829|PDB:4EU9"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:4EU9"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:4EU9"
FT HELIX 117..123
FT /evidence="ECO:0007829|PDB:4EU9"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:4EU9"
FT STRAND 131..139
FT /evidence="ECO:0007829|PDB:4EU9"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:4EU9"
FT HELIX 154..160
FT /evidence="ECO:0007829|PDB:4EU9"
FT STRAND 162..169
FT /evidence="ECO:0007829|PDB:4EU9"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:4EU9"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:4EU9"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:4EU9"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:4EU9"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:4EU9"
FT STRAND 217..223
FT /evidence="ECO:0007829|PDB:4EU9"
FT HELIX 237..255
FT /evidence="ECO:0007829|PDB:4EU9"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:4EU3"
FT HELIX 272..283
FT /evidence="ECO:0007829|PDB:4EU9"
FT STRAND 288..296
FT /evidence="ECO:0007829|PDB:4EU9"
FT HELIX 298..306
FT /evidence="ECO:0007829|PDB:4EU9"
FT STRAND 307..317
FT /evidence="ECO:0007829|PDB:4EU9"
FT HELIX 321..329
FT /evidence="ECO:0007829|PDB:4EU9"
FT HELIX 331..335
FT /evidence="ECO:0007829|PDB:4EU9"
FT STRAND 338..342
FT /evidence="ECO:0007829|PDB:4EU9"
FT HELIX 343..346
FT /evidence="ECO:0007829|PDB:4EU9"
FT HELIX 349..355
FT /evidence="ECO:0007829|PDB:4EU9"
FT STRAND 358..361
FT /evidence="ECO:0007829|PDB:4EU9"
FT STRAND 364..367
FT /evidence="ECO:0007829|PDB:4EU9"
FT STRAND 372..377
FT /evidence="ECO:0007829|PDB:4EU9"
FT TURN 378..380
FT /evidence="ECO:0007829|PDB:4EU9"
FT HELIX 389..395
FT /evidence="ECO:0007829|PDB:4EU9"
FT STRAND 396..402
FT /evidence="ECO:0007829|PDB:4EU9"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:4EU9"
FT TURN 408..411
FT /evidence="ECO:0007829|PDB:4EU9"
FT STRAND 412..418
FT /evidence="ECO:0007829|PDB:4EU9"
FT HELIX 426..428
FT /evidence="ECO:0007829|PDB:4EU9"
FT STRAND 431..434
FT /evidence="ECO:0007829|PDB:4EU9"
FT STRAND 437..440
FT /evidence="ECO:0007829|PDB:4EU9"
FT HELIX 446..456
FT /evidence="ECO:0007829|PDB:4EU9"
FT TURN 460..462
FT /evidence="ECO:0007829|PDB:4EU9"
FT HELIX 463..476
FT /evidence="ECO:0007829|PDB:4EU9"
FT STRAND 478..482
FT /evidence="ECO:0007829|PDB:4EU9"
FT TURN 486..490
FT /evidence="ECO:0007829|PDB:4EU9"
FT HELIX 491..499
FT /evidence="ECO:0007829|PDB:4EU9"
SQ SEQUENCE 505 AA; 54826 MW; C02A8779588D2510 CRC64;
MTERIRNVAL RSKVCPAETA SELIKHGDVV GTSGFTGAGY PKEVPKALAQ RMEAAHDRGE
KYQISLITGA STGPQLDGEL AKANGVYFRS PFNTDATMRN RINAGETEYF DNHLGQVAGR
AVQGNYGKFN IALVEATAIT EDGGIVPTSS VGNSQTFLNL AEKVIIEVNE WQNPMLEGIH
DIWDGNVSGV PTRDIVPIVR ADQRVGGPVL RVNPDKIAAI VRTNDRDRNA PFAAPDETAK
AIAGYLLDFF GHEVKQNRLP PSLLPLQSGV GNVANAVLEG LKEGPFENLV GYSEVIQDGM
LAMLDSGRMR IASASSFSLS PEAAEEINNR MDFFRSKIIL RQQDVSNSPG IIRRLGCIAM
NGMIEADIYG NVNSTRVMGS KMMNGIGGSG DFARSSYLSI FLSPSTAKGG KISAIVPMAA
HVDHIMQDAQ IFVTEQGLAD LRGLSPVQRA REIISKCAHP DYRPMLQDYF DRALKNSFGK
HTPHLLTEAL SWHQRFIDTG TMLPS
