ID   HPCAS_METS5             Reviewed;         661 AA.
AC   A4YGR1;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=3-hydroxypropionyl-coenzyme A synthetase {ECO:0000303|PubMed:18165310};
DE            Short=3-hydroxypropionyl-CoA synthetase {ECO:0000250|UniProtKB:Q973W5};
DE            EC=6.2.1.36;
GN   OrderedLocusNames=Msed_1456;
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] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 186-198, FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND INDUCTION.
RX   PubMed=18165310; DOI=10.1128/jb.01593-07;
RA   Alber B.E., Kung J.W., Fuchs G.;
RT   "3-Hydroxypropionyl-coenzyme A synthetase from Metallosphaera sedula, an
RT   enzyme involved in autotrophic CO2 fixation.";
RL   J. Bacteriol. 190:1383-1389(2008).
CC   -!- FUNCTION: Plays a role in the autotrophic CO(2) fixation pathway.
CC       Activates 3-hydroxypropionate to its CoA ester. Can also activate
CC       propionate, and to a lesser extent acrylate, acetate and butyrate.
CC       {ECO:0000269|PubMed:18165310}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-hydroxypropanoate + ATP + CoA = 3-hydroxypropanoyl-CoA + AMP
CC         + diphosphate; Xref=Rhea:RHEA:26534, ChEBI:CHEBI:16510,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:58528, ChEBI:CHEBI:456215; EC=6.2.1.36;
CC         Evidence={ECO:0000269|PubMed:18165310};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=180 uM for 3-hydroxypropionate {ECO:0000269|PubMed:18165310};
CC         KM=45 uM for ATP {ECO:0000269|PubMed:18165310};
CC       Temperature dependence:
CC         Stable for 15 minutes at up to 80 degrees Celsius.
CC         {ECO:0000269|PubMed:18165310};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:18165310}.
CC   -!- INDUCTION: By autotrophic growth conditions.
CC       {ECO:0000269|PubMed:18165310}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000255}.
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DR   EMBL; CP000682; ABP95613.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4YGR1; -.
DR   SMR; A4YGR1; -.
DR   STRING; 399549.Msed_1456; -.
DR   EnsemblBacteria; ABP95613; ABP95613; Msed_1456.
DR   KEGG; mse:Msed_1456; -.
DR   eggNOG; arCOG01529; Archaea.
DR   HOGENOM; CLU_000022_3_6_2; -.
DR   OMA; AIKASWP; -.
DR   BioCyc; MetaCyc:MON-13728; -.
DR   BRENDA; 6.2.1.17; 7245.
DR   BRENDA; 6.2.1.36; 7245.
DR   Proteomes; UP000000242; Chromosome.
DR   GO; GO:0043955; F:3-hydroxypropionyl-CoA synthetase activity; IDA:UniProtKB.
DR   GO; GO:0003987; F:acetate-CoA ligase activity; IEA:InterPro.
DR   GO; GO:0016208; F:AMP binding; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:InterPro.
DR   GO; GO:0043427; P:carbon fixation by 3-hydroxypropionate cycle; IDA:UniProtKB.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   InterPro; IPR011904; Ac_CoA_lig.
DR   InterPro; IPR032387; ACAS_N.
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; PF16177; ACAS_N; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   TIGRFAMs; TIGR02188; Ac_CoA_lig_AcsA; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Direct protein sequencing; Ligase;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..661
FT                   /note="3-hydroxypropionyl-coenzyme A synthetase"
FT                   /id="PRO_0000403054"
FT   ACT_SITE        526
FT                   /evidence="ECO:0000250|UniProtKB:Q8ZKF6"
FT   MOD_RES         617
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8ZKF6"
SQ   SEQUENCE   661 AA;  74402 MW;  58CE732AF5E9A27A CRC64;
     MFMRYIMVEE QTLKTGSQEL EEKADYNMRY YAHLMKLSKE KPAEFWGSLA QDLLDWYEPW
     KETMRQEDPM TRWFIGGKIN ASYNAVDRHL NGPRKFKAAV IWESELGERK IVTYQDMFYE
     VNRWANALRS LGVGKGDRVT IYMPLTPEGI AAMLASARIG AIHSVIFAGF GSQAIADRVE
     DAKAKVVITA DAYPRRGKVV ELKKTVDEAL NSLGERSPVQ HVLVYRRMKT DVNMKEGRDV
     FFDEVGKYRY VEPERMDSND PLFILYTSGT TGKPKGIMHS TGGYLTGTAV MLLWSYGLSQ
     ENDVLFNTSD IGWIVGHSYI TYSPLIMGRT VVIYESAPDY PYPDKWAEII ERYRATTFGT
     SATALRYFMK YGDEYVKNHD LSSIRIIVTN GEVLNYSPWK WGLEVLGGGK VFMSHQWWQT
     ETGAPNLGYL PGIIYMPMKS GPASGFPLPG NFVEVLDENG NPSAPRVRGY LVMRPPFPPN
     MMMGMWNDNG ERLKKTYFSK FGSLYYPGDF AMVDEDGYIW VLGRADETLK IAAHRIGAGE
     VESAITSHPS VAEAAVIGVP DSVKGEEVHA FVVLKQGYAP SSELAKDIQS HVRKVMGPIV
     SPQIHFVDKL PKTRSGKVMR RVIKAVMMGS SAGDLTTIED EASMDEIKKA VEELKKELKT
     S