HBCAL_NITMS
ID HBCAL_NITMS Reviewed; 698 AA.
AC A9A1Y1;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=4-hydroxybutyrate--CoA ligase [ADP-forming] {ECO:0000305};
DE EC=6.2.1.56 {ECO:0000269|PubMed:24843170};
DE AltName: Full=4-hydroxybutyryl-coenzyme A synthetase [ADP-forming] {ECO:0000305};
DE Short=4-hydroxybutyryl-CoA synthetase [ADP-forming] {ECO:0000303|PubMed:24843170};
GN OrderedLocusNames=Nmar_0206 {ECO:0000312|EMBL:ABX12102.1};
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 4-hydroxybutyryl-CoA, ADP and
CC phosphate from 4-hydroxybutyrate, coenzyme A (CoA) and ATP. Can also
CC use acetate, propionate and butyrate, with poor catalytic efficiency.
CC {ECO:0000269|PubMed:24843170}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxybutanoate + ATP + CoA = 4-hydroxybutanoyl-CoA + ADP +
CC phosphate; Xref=Rhea:RHEA:58896, ChEBI:CHEBI:16724,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:58574, ChEBI:CHEBI:456216; EC=6.2.1.56;
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=0.37 mM for 4-hydroxybutyrate {ECO:0000269|PubMed:24843170};
CC KM=200 mM for acetate {ECO:0000269|PubMed:24843170};
CC KM=88 mM for propionate {ECO:0000269|PubMed:24843170};
CC KM=5 mM for butyrate {ECO:0000269|PubMed:24843170};
CC KM=0.22 mM for ATP {ECO:0000269|PubMed:24843170};
CC KM=0.16 mM for CoA {ECO:0000269|PubMed:24843170};
CC Vmax=1.4 umol/min/mg enzyme with 4-hydroxybutyrate as substrate
CC {ECO:0000269|PubMed:24843170};
CC Vmax=0.22 umol/min/mg enzyme with acetate as substrate
CC {ECO:0000269|PubMed:24843170};
CC Vmax=0.10 umol/min/mg enzyme with propionate as substrate
CC {ECO:0000269|PubMed:24843170};
CC Vmax=0.61 umol/min/mg enzyme with butyrate as substrate
CC {ECO:0000269|PubMed:24843170};
CC Vmax=1.7 umol/min/mg enzyme with ATP as substrate
CC {ECO:0000269|PubMed:24843170};
CC Vmax=1.4 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 alpha subunit family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the acetate CoA
CC ligase beta subunit family. {ECO:0000305}.
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DR EMBL; CP000866; ABX12102.1; -; Genomic_DNA.
DR AlphaFoldDB; A9A1Y1; -.
DR SMR; A9A1Y1; -.
DR STRING; 436308.Nmar_0206; -.
DR EnsemblBacteria; ABX12102; ABX12102; Nmar_0206.
DR KEGG; nmr:Nmar_0206; -.
DR eggNOG; arCOG01340; Archaea.
DR HOGENOM; CLU_007415_3_1_2; -.
DR OMA; SFMSQSG; -.
DR PhylomeDB; A9A1Y1; -.
DR BioCyc; MetaCyc:MON-20107; -.
DR BRENDA; 6.2.1.56; 10773.
DR Proteomes; UP000000792; Chromosome.
DR GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; 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; IPR043938; Ligase_CoA_dom.
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; PF19045; Ligase_CoA_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..698
FT /note="4-hydroxybutyrate--CoA ligase [ADP-forming]"
FT /id="PRO_0000453089"
FT DOMAIN 491..544
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 517..544
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
SQ SEQUENCE 698 AA; 75619 MW; 1A89F457B276F758 CRC64;
MTDSPILSPK SIAVIGASDK RGSVGATITS NIMNGFKGTV YPISPTRDTV FYKKAYKSVL
DVPKSIDLAV IVIKNTLVTP VLEECGKKKI KGVIIITAGF KEVDEEGAKR EQQVIDIAKK
YNMQVVGPNC LGVMNLDSKT MMNSTFLKVT PKSGKIALVS QSGAICAALV EDASAQGIGF
SAVVSLGNKA VMSEVDVLKI LANHKQTEVI VMYLEDMGDG QEFLKVCKNI TKKLKKPVLV
LKSGRSPEGA KAAMSHTGAL MGSDEIYDAL LKQSGAIRVD TMEELFDYAT AFSKQPLPSN
GDLVIVSNAG GPAIISTDAC SKAKIKMADI TSIRKKIDEV IPPWGSSRNP VDIVGDADFN
RFHNVLDRVL KHPKVGSVIS MCTPSGTLNY DKLAEVIVEM SKKYKKTMLA SLMGLDEGVT
NREILADGNV PYYTYAEGAI RTLAAMIRFS DWVKSSPGKI TKFKVNKAKA KKIFDQVKKE
KRPNLLEEEG QEVLKAYGLP LPKSTLAKNE AEAVKAAKKI GYPVVMKIAS PQIIHKSDAG
GVKVNLTNDA EVKDAFKTIV KNAKKYNKKA EIKGVLIVEM VKGGKELIIG SKLEPGFGPV
IMLGMGGIYV EVLKDVTFKL APVTDKEADD MIASIKTQKL LQGVRGEKPS DIVKLSECIQ
RLSQLVSDFK EIKELDMNPV LVMEKGKGCR ILDVRIGL
