ID H5SJB9_9BACT Unreviewed; 712 AA.
AC H5SJB9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 13-SEP-2023, entry version 22.
DE SubName: Full=CoA-binding domain-containing protein {ECO:0000313|EMBL:BAL56255.1};
GN ORFNames=HGMM_F35G12C26 {ECO:0000313|EMBL:BAL56255.1}, HGMM_F51D07C07
GN {ECO:0000313|EMBL:BAL57526.1};
OS uncultured Acetothermia bacterium.
OC Bacteria; Candidatus Bipolaricaulota; environmental samples.
OX NCBI_TaxID=236499 {ECO:0000313|EMBL:BAL56255.1};
RN [1] {ECO:0000313|EMBL:BAL56255.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16309394; DOI=10.1111/j.1462-2920.2005.00881.x;
RA Nunoura T., Hirayama H., Takami H., Oida H., Nishi S., Shimamura S.,
RA Suzuki Y., Inagaki F., Takai K., Nealson K.H., Horikoshi K.;
RT "Genetic and functional properties of uncultivated thermophilic
RT crenarchaeotes from a subsurface gold mine as revealed by analysis of
RT genome fragments.";
RL Environ. Microbiol. 7:1967-1984(2005).
RN [2] {ECO:0000313|EMBL:BAL56255.1}
RP NUCLEOTIDE SEQUENCE.
RA Takami H., Noguchi H., Takaki Y., Uchiyama I., Toyoda A., Nishi S.,
RA Chee G.-J., Arai W., Nunoura T., Itoh T., Hattori M., Takai K.;
RT "A Deeply Branching Thermophilic Bacterium with an Ancient Acetyl-CoA
RT Pathway Dominates a Subsurface Ecosystem.";
RL PLoS ONE 7:e30559-e30559(2012).
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DR EMBL; AP011741; BAL56255.1; -; Genomic_DNA.
DR EMBL; AP011778; BAL57526.1; -; Genomic_DNA.
DR AlphaFoldDB; H5SJB9; -.
DR GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 2.
DR InterPro; IPR014089; AcCoA-synth-alpha.
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 NCBIfam; TIGR02717; AcCoA-syn-alpha; 1.
DR PANTHER; PTHR43334; ACETATE--COA LIGASE [ADP-FORMING]; 1.
DR PANTHER; PTHR43334:SF1; ACETATE--COA LIGASE [ADP-FORMING]; 1.
DR Pfam; PF13549; ATP-grasp_5; 1.
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; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 2.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 504..540
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 712 AA; 77736 MW; CEBD3C64DBD82C20 CRC64;
MTTHSPESLR ALFAPKSVAV IGASTKPDSL GRVVFKNILF YGYTGVVYPV NPKAHSILGV
KAYPSVLDIP DEIDLAVIIV PALAVASVLD ECGRKGVRAA IIISAGFKEI GEEGAKRELE
LQQIAQRYGI ALLGPNCLGL INTDPHVSLN ATFAPGMPRQ GNIAFISQSG ALGVAALEYA
QRQKIGLSKF ISIGNKADLH ENHLLEYLKD DPLSDVILLY VEDLEDPQEF HKLATEITSE
RAKKIPILAI KSGRTLEGAK AATSHTGALA GSDEVYDSVF MQSGVLRVET IEELFDYAVA
FAQQPLPKGN KIAIVTNAGG AGILATDAAV RYGLQLASFT EETVKRLREL LPPTVSVGNP
VDMTGEPNES RYETIVRTVL ADPNVNGVIV IAAPHILMSL ENIARNIVRA VQETNTEKPV
LACLMAVTDA RPAIEILEAI NIPNYSFPER AARALAAMAR YHDWVHRPRT EYKVFTDIQI
ERAREIIAHA KRDGRRLLLE PEAHDLLKAY GFPVLKYRLA KSEAEALQAA HEIGYPVVLK
IVSPDIVHKV DVGGVKLDIH NDAELRESYR QMLAHVTQAK PSAQIAGVFV QEFVQGGKET
ILGLKRDPLF GPLLMFGLGG IYVEALRDVT FRLAPVRELG IQRMIRQIRG FRILEGFRGE
LPSDIDAIAE CLARLSQLAT QIEEIVELDI NPLIVLERGR GARVVDARIV VA
//