HPCAL_NITMS
ID HPCAL_NITMS Reviewed; 705 AA.
AC A9A2G6;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=3-hydroxypropionate--CoA ligase [ADP-forming] {ECO:0000305};
DE EC=6.2.1.- {ECO:0000269|PubMed:24843170};
DE AltName: Full=3-hydroxypropionyl-coenzyme A synthetase [ADP-forming] {ECO:0000305};
DE Short=3-hydroxypropionyl-CoA synthetase [ADP-forming] {ECO:0000303|PubMed:24843170};
GN OrderedLocusNames=Nmar_1309 {ECO:0000312|EMBL:ABX13205.1};
OS Nitrosopumilus maritimus (strain SCM1).
OC Archaea; Thaumarchaeota; Nitrosopumilales; Nitrosopumilaceae;
OC Nitrosopumilus.
OX NCBI_TaxID=436308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCM1;
RX PubMed=20421470; DOI=10.1073/pnas.0913533107;
RA Walker C.B., de la Torre J.R., Klotz M.G., Urakawa H., Pinel N., Arp D.J.,
RA Brochier-Armanet C., Chain P.S., Chan P.P., Gollabgir A., Hemp J.,
RA Hugler M., Karr E.A., Konneke M., Shin M., Lawton T.J., Lowe T.,
RA Martens-Habbena W., Sayavedra-Soto L.A., Lang D., Sievert S.M.,
RA Rosenzweig A.C., Manning G., Stahl D.A.;
RT "Nitrosopumilus maritimus genome reveals unique mechanisms for
RT nitrification and autotrophy in globally distributed marine crenarchaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:8818-8823(2010).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=SCM1;
RX PubMed=24843170; DOI=10.1073/pnas.1402028111;
RA Koenneke M., Schubert D.M., Brown P.C., Huegler M., Standfest S.,
RA Schwander T., Schada von Borzyskowski L., Erb T.J., Stahl D.A., Berg I.A.;
RT "Ammonia-oxidizing archaea use the most energy-efficient aerobic pathway
RT for CO2 fixation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:8239-8244(2014).
CC -!- FUNCTION: Involved in thaumarchaeal hydroxypropionate/hydroxybutyrate
CC (HP/HB) cycle, a modified version of the autotrophic HP/HB cycle of
CC Crenarchaeota. Catalyzes the formation of 3-hydroxypropionyl-CoA, ADP
CC and phosphate from 3-hydroxypropionate, coenzyme A (CoA) and ATP. Can
CC also use 4-hydroxybutyrate, propionate and butyrate, with poor
CC catalytic efficiency. {ECO:0000269|PubMed:24843170}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxypropanoate + ATP + CoA = 3-hydroxypropanoyl-CoA + ADP
CC + phosphate; Xref=Rhea:RHEA:67136, ChEBI:CHEBI:16510,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:58528, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:24843170};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:24843170};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:24843170};
CC Note=No activity with Ni(2+), Co(2+) and Ca(2+).
CC {ECO:0000269|PubMed:24843170};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.2 mM for 3-hydroxypropionate {ECO:0000269|PubMed:24843170};
CC KM=5.6 mM for 4-hydroxybutyrate {ECO:0000269|PubMed:24843170};
CC KM=17.0 mM for propionate {ECO:0000269|PubMed:24843170};
CC KM=12.4 mM for butyrate {ECO:0000269|PubMed:24843170};
CC KM=0.6 mM for ATP {ECO:0000269|PubMed:24843170};
CC KM=0.16 mM for CoA {ECO:0000269|PubMed:24843170};
CC Vmax=0.59 umol/min/mg enzyme with 3-hydroxypropionate as substrate
CC {ECO:0000269|PubMed:24843170};
CC Vmax=0.48 umol/min/mg enzyme with 4-hydroxybutyrate as substrate
CC {ECO:0000269|PubMed:24843170};
CC Vmax=0.50 umol/min/mg enzyme with propionate as substrate
CC {ECO:0000269|PubMed:24843170};
CC Vmax=0.54 umol/min/mg enzyme with butyrate as substrate
CC {ECO:0000269|PubMed:24843170};
CC Vmax=0.59 umol/min/mg enzyme with ATP as substrate
CC {ECO:0000269|PubMed:24843170};
CC Vmax=0.60 umol/min/mg enzyme with CoA as substrate
CC {ECO:0000269|PubMed:24843170};
CC -!- SIMILARITY: In the N-terminal section; belongs to the acetate CoA
CC ligase beta subunit family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the acetate CoA
CC ligase alpha subunit family. {ECO:0000305}.
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DR EMBL; CP000866; ABX13205.1; -; Genomic_DNA.
DR AlphaFoldDB; A9A2G6; -.
DR SMR; A9A2G6; -.
DR STRING; 436308.Nmar_1309; -.
DR EnsemblBacteria; ABX13205; ABX13205; Nmar_1309.
DR KEGG; nmr:Nmar_1309; -.
DR eggNOG; arCOG01338; Archaea.
DR eggNOG; arCOG01340; Archaea.
DR HOGENOM; CLU_007415_2_2_2; -.
DR OMA; CNFNPPE; -.
DR PhylomeDB; A9A2G6; -.
DR Proteomes; UP000000792; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.40.50.261; -; 2.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR003781; CoA-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032875; Succ_CoA_lig_flav_dom.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR Pfam; PF13380; CoA_binding_2; 1.
DR Pfam; PF13607; Succ_CoA_lig; 1.
DR SMART; SM00881; CoA_binding; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF52210; SSF52210; 2.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Ligase; Magnesium; Manganese; Metal-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..705
FT /note="3-hydroxypropionate--CoA ligase [ADP-forming]"
FT /id="PRO_0000453090"
FT DOMAIN 25..61
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 51..61
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
SQ SEQUENCE 705 AA; 76129 MW; 2B8C043794C85FAC CRC64;
MAAVKKIFDE IIETDHKVIT EESSKSILKN YGVKVPPYAL VTSAEEAAKE AKKIGFPLVM
KVVSPQILHK TDVGGVKVGL DNVADVKKTF TDMYGRLSKK KGVNVKGILL EKMVPKGVEL
IVGIQNDSQF GPIIMVGMGG IMTEVMKDVA FRMLPITTSD AKSMLNELKG SKLLKGFRGS
EPIDTNLVAK MLVNIGKLGV ENADYINSID FNPVIVYPKS HYVVDAKIIL NKEKKKNSIS
KAKPSITDME TFFTPKSVAL VGASASPGKI GNSILDSLVN YDFKGKVYPI NPKADKIFGQ
KCYPSVADIP GKVDLVVVSV DLSMTPPVLE DCAKKGVHSV VIVSGGGKEL GGERAAYEAE
VARLSKKHKI RIIGPNCIGM FNAANRLDCA FQGQERMVRS KLGPVAFFSQ SGTMGISMLE
SADTFGLSKM ISFGNRSDVD EADMIWYAAN DPQTKVIGLY VEGFGDGRKF INVAKRVMKE
KKKPIVIWKS GRTAAGAKQA ASHTGSLGGS NAIIMGAFKQ AGIISVDSYQ ELAGVLKALA
WQPAAKGNKV AMTSNGAGPM IGGIDQLEKF GLAIGKLSPK LLKKMKSRFP PAVPIHNGNP
ADVGGGATAD DYQFVIQQFM DEKNIDIAMP WFVFQDDPLE ETIVDHLAGF QKKAKKPLLC
GGNGGPYTEK MIKLIEKHNV PVYQDLRTWV AAASALHQWG KISKK
