ID   HPCAS_SULTO             Reviewed;         659 AA.
AC   Q973W5; B8XVT0;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=3-hydroxypropionyl-coenzyme A synthetase {ECO:0000303|PubMed:18165310};
DE            Short=3-hydroxypropionyl-CoA synthetase {ECO:0000312|EMBL:ACJ71674.1};
DE            EC=6.2.1.36;
GN   OrderedLocusNames=STK_07830;
OS   Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS   (Sulfolobus tokodaii).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfurisphaera.
OX   NCBI_TaxID=273063;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:ACJ71674.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
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).
RN   [2] {ECO:0000312|EMBL:BAB65795.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX   PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA   Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA   Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA   Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA   Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT   "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT   Sulfolobus tokodaii strain7.";
RL   DNA Res. 8:123-140(2001).
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=190 uM for 3-hydroxypropionate {ECO:0000269|PubMed:18165310};
CC         KM=110 uM for ATP {ECO:0000269|PubMed:18165310};
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000255}.
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DR   EMBL; FJ445416; ACJ71674.1; -; Genomic_DNA.
DR   EMBL; BA000023; BAB65795.1; -; Genomic_DNA.
DR   RefSeq; WP_010978778.1; NC_003106.2.
DR   AlphaFoldDB; Q973W5; -.
DR   SMR; Q973W5; -.
DR   STRING; 273063.STK_07830; -.
DR   PRIDE; Q973W5; -.
DR   EnsemblBacteria; BAB65795; BAB65795; STK_07830.
DR   GeneID; 1458745; -.
DR   KEGG; sto:STK_07830; -.
DR   PATRIC; fig|273063.9.peg.881; -.
DR   eggNOG; arCOG01529; Archaea.
DR   OMA; AIKASWP; -.
DR   OrthoDB; 24323at2157; -.
DR   BRENDA; 6.2.1.36; 15396.
DR   Proteomes; UP000001015; 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; Ligase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..659
FT                   /note="3-hydroxypropionyl-coenzyme A synthetase"
FT                   /id="PRO_0000403055"
FT   ACT_SITE        525
FT                   /evidence="ECO:0000250|UniProtKB:Q8ZKF6"
FT   MOD_RES         616
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8ZKF6"
FT   CONFLICT        518
FT                   /note="I -> L (in Ref. 1; ACJ71674)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   659 AA;  74106 MW;  355BEB88D03D3CEC CRC64;
     MTEKLSEQLQ QLGEQNLEEK ADYNMRYYKY LYKKSIEEPD KFWGELAEEL ITWYEPWKQA
     FVQEEGLLTK WFVGGKLNAS YNAVDRHLNS HRKYKAAIFW ESEKGEKKVV TYQDLFYEVN
     KWANALRELG VKKGDRVTIY MPLTPEGVIA KLAVARLGAI HSVVFAGFGA QALADRIADA
     GAKVVITADA YYRRGKLVEL KKTVDEALNI LGDKSPVQKV LVYKRTGTEI PFKEGRDVYF
     DEVGKYKYIE PVPVEATEPL FILYTSGTTG KPKGIVHSTG GYLVGTAVML LWSYGLSQEN
     DVLFNTSDIG WIVGHSYITY SPLVMGRSIV IYESAPDYPY PDKWAEMIEK YRATTFGTSA
     TAIRTLMKYG EDYVKQHDLS SLRIIVTNGE PLNYAPWKWG LEVVGGGKVF MSHQWWQTET
     GGPNIGYIPG VVYLPMKSGP AVGFALPGNK VTVVNEEGKE TKPRERGYLV MLPPFPPMMM
     IGMWNDPDNE RLKKTYFSKF PGIYYPGDYA MIDEDGYIWV MGRADETIKV AAHRIGAGEV
     ESIVTSHPAV AEAAAVGIPD PVKGEAVHLF VVLKVGYKPS PQLAREIQEH VRKYMGAIVT
     PEVHFVDKLP KTRSGKIMRR VIKAVMMGQS AGDITTLEDE ASMDEIKKAV EEFKKSLSQ