ID A0A0S8HW66_9CHLR Unreviewed; 696 AA.
AC A0A0S8HW66;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=CoA-binding protein {ECO:0000313|EMBL:KPK89539.1};
GN ORFNames=AMJ88_17410 {ECO:0000313|EMBL:KPK89539.1};
OS Anaerolineae bacterium SM23_ 63.
OC Bacteria; Chloroflexota; Anaerolineae.
OX NCBI_TaxID=1703387 {ECO:0000313|EMBL:KPK89539.1, ECO:0000313|Proteomes:UP000051685};
RN [1] {ECO:0000313|EMBL:KPK89539.1, ECO:0000313|Proteomes:UP000051685}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_ 63 {ECO:0000313|EMBL:KPK89539.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPK89539.1}.
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DR EMBL; LJUS01000113; KPK89539.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8HW66; -.
DR PATRIC; fig|1703387.3.peg.2387; -.
DR Proteomes; UP000051685; Unassembled WGS sequence.
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; 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 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 492..579
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 696 AA; 75249 MW; EF0842757FC2D830 CRC64;
MLDVLFRPKS VAVIGASTKE LSIGNRIVKN LIDFGFKGSI YPISLKSDEI LGVKAYKSIL
EVPGDIDVVH MVIPSKFVPQ AIDDCGDKGV KFVILNGGGF AEVGPEGAAI EEDCLVRAKA
HGIRILGPNC QGIINTDPDV RAYCNFTFTK PDPGSISIVA LSGGVAETIH QAFSEMGIGT
RMYASNGNAC DITIPEILNY YGDDEGTRVI LLYVEGLRDP EAFLKAASEV AAKKPILAMK
AGRTEEGAKA AASHTGGLAK VDLATDLIFE KTGILSFTDE AELCHAAVAF SSQPIPKGNR
VGMITNTGGP AVIATDVFVN AGMEIPPLSK KAEAILQEKL FPEASVGNPI DVLATAGAEQ
FRTAIDVIMD EDQLDSVYIN FVTPFFVDAE SIAREIVEVN QESKKPIICN LMTDKRQWKG
TVDILKEGGV PYYSFPSTAA KVLTALTKYH EIRTREIGEA RRFEDVDREN VAAILQKAKG
AGREWLSATE VYQILGAYGI PTADWQVTTN SEEAVKAAAE IDFPVVVKVD ADTIVHKSDV
GGVVVDLWDN DAVRSTVEEM EERLNTKDLR FLIQKYLPGG KEIIIGAKAE EGLGHLVMFG
IGGIYVEIMK DVIFKLTPVT TVEAHEMISS LQAAPLLRGI RGGKGVNQER IVEIIQRVSQ
LVSDCPTIQE LDLNPIIAYE DQVLVVDARI FIANSH
//
