HBCL1_METS5
ID HBCL1_METS5 Reviewed; 564 AA.
AC A4YDT1;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=4-hydroxybutyrate--CoA ligase 1 {ECO:0000303|PubMed:23258541};
DE EC=6.2.1.40 {ECO:0000269|PubMed:23258541};
DE AltName: Full=Acetate--CoA ligase {ECO:0000305|PubMed:23258541};
DE EC=6.2.1.1 {ECO:0000269|PubMed:23258541};
DE AltName: Full=Butyrate--CoA ligase {ECO:0000305|PubMed:23258541};
DE EC=6.2.1.2 {ECO:0000269|PubMed:23258541};
DE AltName: Full=Propionate--CoA ligase {ECO:0000305|PubMed:23258541};
DE EC=6.2.1.17 {ECO:0000269|PubMed:23258541};
GN OrderedLocusNames=Msed_0406;
OS Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509
OS / TH2).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Metallosphaera.
OX NCBI_TaxID=399549;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2;
RX PubMed=18083856; DOI=10.1128/aem.02019-07;
RA Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.;
RT "The genome sequence of the metal-mobilizing, extremely thermoacidophilic
RT archaeon Metallosphaera sedula provides insights into bioleaching-
RT associated metabolism.";
RL Appl. Environ. Microbiol. 74:682-692(2008).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE
RP SPECIFICITY.
RC STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2;
RX PubMed=23258541; DOI=10.1074/jbc.m112.413195;
RA Hawkins A.S., Han Y., Bennett R.K., Adams M.W., Kelly R.M.;
RT "Role of 4-hydroxybutyrate-CoA synthetase in the CO2 fixation cycle in
RT thermoacidophilic archaea.";
RL J. Biol. Chem. 288:4012-4022(2013).
CC -!- FUNCTION: Involved in the 3-hydroxypropionate/4-hydroxybutyrate cycle
CC which incorporates carbon dioxide into cellular carbon. Catalyzes the
CC ligation of coenzyme A (CoA) to 4-hydroxybutyrate (4HB). It can also
CC use butyrate, valerate, propionate, acetate and 3-hydroxybutyrate (3HB)
CC as substrates. {ECO:0000269|PubMed:23258541}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxybutanoate + ATP + CoA = 4-hydroxybutanoyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:23128, ChEBI:CHEBI:16724,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:58574, ChEBI:CHEBI:456215; EC=6.2.1.40;
CC Evidence={ECO:0000269|PubMed:23258541};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate;
CC Xref=Rhea:RHEA:23176, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:456215; EC=6.2.1.1;
CC Evidence={ECO:0000269|PubMed:23258541};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + propanoate = AMP + diphosphate + propanoyl-CoA;
CC Xref=Rhea:RHEA:20373, ChEBI:CHEBI:17272, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57392,
CC ChEBI:CHEBI:456215; EC=6.2.1.17;
CC Evidence={ECO:0000269|PubMed:23258541};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a medium chain fatty acid + ATP + CoA = a medium-chain fatty
CC acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:48340,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:59558, ChEBI:CHEBI:90546, ChEBI:CHEBI:456215; EC=6.2.1.2;
CC Evidence={ECO:0000269|PubMed:23258541};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q08AH3};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q08AH3};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=320 uM for butyrate {ECO:0000269|PubMed:23258541};
CC KM=380 uM for propionate {ECO:0000269|PubMed:23258541};
CC KM=740 uM for valerate {ECO:0000269|PubMed:23258541};
CC KM=810 uM for 3HB {ECO:0000269|PubMed:23258541};
CC KM=2000 uM for 4HB {ECO:0000269|PubMed:23258541};
CC KM=2030 uM for acetate {ECO:0000269|PubMed:23258541};
CC Vmax=15.1 umol/min/mg enzyme with propionate as substrate
CC {ECO:0000269|PubMed:23258541};
CC Vmax=7.9 umol/min/mg enzyme with butyrate as substrate
CC {ECO:0000269|PubMed:23258541};
CC Vmax=6 umol/min/mg enzyme with acetate as substrate
CC {ECO:0000269|PubMed:23258541};
CC Vmax=5.2 umol/min/mg enzyme with valerate as substrate
CC {ECO:0000269|PubMed:23258541};
CC Vmax=2.4 umol/min/mg enzyme with 3HB as substrate
CC {ECO:0000269|PubMed:23258541};
CC Vmax=1.7 umol/min/mg enzyme with 4HB as substrate
CC {ECO:0000269|PubMed:23258541};
CC Note=kcat is 16.2 sec(-1) for ligase activity with propionate as
CC substrate. kcat is 8.4 sec(-1) for ligase activity with butyrate as
CC substrate. kcat is 6.4 sec(-1) for ligase activity with acetate as
CC substrate. kcat is 5.6 sec(-1) for ligase activity with valerate as
CC substrate. kcat is 2.6 sec(-1) for ligase activity with 3HB as
CC substrate. kcat is 1.8 sec(-1) for ligase activity with 4HB as
CC substrate. {ECO:0000269|PubMed:23258541};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; CP000682; ABP94583.1; -; Genomic_DNA.
DR RefSeq; WP_012020371.1; NC_009440.1.
DR AlphaFoldDB; A4YDT1; -.
DR SMR; A4YDT1; -.
DR STRING; 399549.Msed_0406; -.
DR EnsemblBacteria; ABP94583; ABP94583; Msed_0406.
DR GeneID; 5105523; -.
DR GeneID; 59456144; -.
DR KEGG; mse:Msed_0406; -.
DR eggNOG; arCOG04201; Archaea.
DR HOGENOM; CLU_000022_59_10_2; -.
DR OMA; HAWSNLF; -.
DR BioCyc; MetaCyc:MON-13735; -.
DR BRENDA; 6.2.1.40; 7245.
DR Proteomes; UP000000242; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003987; F:acetate-CoA ligase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0047760; F:butyrate-CoA ligase activity; IDA:UniProtKB.
DR GO; GO:0031956; F:medium-chain fatty acid-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0050218; F:propionate-CoA ligase activity; IDA:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Fatty acid metabolism; Ligase; Lipid metabolism; Magnesium;
KW Membrane; Nucleotide-binding; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..564
FT /note="4-hydroxybutyrate--CoA ligase 1"
FT /id="PRO_0000435708"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 204..212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 343..348
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 348
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 429
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 444
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 452..454
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 455
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 484
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 513
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 521..523
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 538
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
SQ SEQUENCE 564 AA; 64307 MW; 662037C59B411AE6 CRC64;
MVTVQDFFRK FIEFQNSPNE KSLQEIVKLV GQLDLRRFNW VRDVFEDIHV KERGSKTALI
WRDINTGEEA KLSYHELSLM SNRVLSTLRK HGLKKGDVVY LMTKVHPMHW AVFLAVIKGG
FVMVPSATNL TVAEMKYRFS DLKPSAIISD SLRASVMEEA LGSLKVEKFL IDGKRETWNS
LEDESSNAEP EDTRGEDVII NYFTSGTTGM PKRVIHTAVS YPVGSITTAS IVGVRESDLH
LNLSATGWAK FAWSSFFSPL LVGATVVGIN YEGKLDTRRY LGEVENLGVT SFCAPPTAWR
QFITLDLDQF RFERLRSVVS AGEPLNPEVI KIWKDKFNLT IRDFYGQTET TAMVGNFPFL
KVKPGSMGKP HPLYDIRLLD DEGKEITKPY EVGHITVKLN PRPIGLFLGY SDEKKNMESF
REGYYYTGDK AYFDEEGYFY FVGRGDDVIK TSDYRVGPFE VESALLEHPA VAEAAVVGVP
DTVRWQLVKA YIVLKKGYMP SKELAEEIRE KMKTLLSPYK VPRIIEFVDE LPKTISGKIR
RVELRKREEE KRKKGEVGQN EYVF
