HBCL2_METS5
ID HBCL2_METS5 Reviewed; 549 AA.
AC A4YDR9;
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 2 {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};
DE AltName: Full=acyl-activating enzyme;
GN OrderedLocusNames=Msed_0394;
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: Catalyzes the ligation of coenzyme A (CoA) to 4-
CC hydroxybutyrate (4HB). It can also use butyrate, valerate, propionate,
CC acetate and 3-hydroxybutyrate (3HB) as substrates.
CC {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=60 uM for butyrate {ECO:0000269|PubMed:23258541};
CC KM=120 uM for valerate {ECO:0000269|PubMed:23258541};
CC KM=540 uM for propionate {ECO:0000269|PubMed:23258541};
CC KM=680 uM for acetate {ECO:0000269|PubMed:23258541};
CC KM=1540 uM for 4HB {ECO:0000269|PubMed:23258541};
CC KM=1880 uM for 3HB {ECO:0000269|PubMed:23258541};
CC Vmax=0.22 umol/min/mg enzyme with 4HB as substrate
CC {ECO:0000269|PubMed:23258541};
CC Vmax=0.21 umol/min/mg enzyme with butyrate as substrate
CC {ECO:0000269|PubMed:23258541};
CC Vmax=0.20 umol/min/mg enzyme with valerate as substrate
CC {ECO:0000269|PubMed:23258541};
CC Vmax=0.20 umol/min/mg enzyme with propionate as substrate
CC {ECO:0000269|PubMed:23258541};
CC Vmax=0.13 umol/min/mg enzyme with acetate as substrate
CC {ECO:0000269|PubMed:23258541};
CC Vmax=0.07 umol/min/mg enzyme with 3HB as substrate
CC {ECO:0000269|PubMed:23258541};
CC Note=kcat is 0.24 sec(-1) for ligase activity with 4HB as substrate.
CC kcat is 0.23 sec(-1) for ligase activity with butyrate as substrate.
CC kcat is 0.22 sec(-1) for ligase activity with valerate as substrate.
CC kcat is 0.21 sec(-1) for ligase activity with propionate as
CC substrate. kcat is 0.14 sec(-1) for ligase activity with acetate as
CC substrate. kcat is 0.08 sec(-1) for ligase activity with 3HB as
CC substrate. {ECO:0000269|PubMed:23258541};
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; CP000682; ABP94571.1; -; Genomic_DNA.
DR RefSeq; WP_012020359.1; NC_009440.1.
DR AlphaFoldDB; A4YDR9; -.
DR SMR; A4YDR9; -.
DR STRING; 399549.Msed_0394; -.
DR PRIDE; A4YDR9; -.
DR EnsemblBacteria; ABP94571; ABP94571; Msed_0394.
DR GeneID; 5103637; -.
DR GeneID; 59456160; -.
DR KEGG; mse:Msed_0394; -.
DR eggNOG; arCOG00856; Archaea.
DR HOGENOM; CLU_000022_59_5_2; -.
DR OMA; YGPGTFC; -.
DR BRENDA; 6.2.1.40; 7245.
DR Proteomes; UP000000242; Chromosome.
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; IPR020845; AMP-binding_CS.
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.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Fatty acid metabolism; Ligase; Lipid metabolism; Magnesium;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..549
FT /note="4-hydroxybutyrate--CoA ligase 2"
FT /id="PRO_0000435709"
FT BINDING 195..203
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 336..341
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 425
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 440
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 448..450
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 506
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 514..516
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 530
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
SQ SEQUENCE 549 AA; 62011 MW; 31D61ED874513B53 CRC64;
MGGFKIPNYE GVDPTGSWYS VLTPLLFLER AGKYFKDKTA VVYRDSRYTY STFYDNVMVQ
ASALMRRGFS REDKLSFISR NRPEFLESFF GVPYAGGVLV PINFRLSPKE MAYIINHSDS
KFVVVDEPYL NSLLEVKDQI KAEIILLEDP DNPSASETAR KEVRMTYREL VKGGSRDPLP
IPAKEEYSMI TLYYTSGTTG LPKGVMHHHR GAFLNAMAEV LEHQMDLNSV YLWTLPMFHA
ASWGFSWATV AVGATNVCLD KVDYPLIYRL VEKERVTHMC AAPTVYVNLA DYMKRNNLKF
SNRVHMLVAG AAPAPATLKA MQEIGGYMCH VYGLTETYGP HSICEWRREW DSLPLEEQAK
LKARQGIPYV SFEMDVFDAN GKPVPWDGKT IGEVVMRGHN VALGYYKNPE KTAESFRDGW
FHSGDAAVVH PDGYIEIVDR FKDLINTGGE KVSSILVEKT LMEIPGVKAV AVYGTPDEKW
GEVVTARIEL QEGVKLTEEE VIKFCKERLA HFECPKIVEF GPIPMTATGK MQKYVLRNEA
KAKANKEKS
