ID A0A0S8C9K9_9PROT Unreviewed; 707 AA.
AC A0A0S8C9K9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=CoA-binding domain-containing protein {ECO:0000259|SMART:SM00881};
GN ORFNames=AMJ67_00625 {ECO:0000313|EMBL:KPK20505.1};
OS Betaproteobacteria bacterium SG8_41.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1703391 {ECO:0000313|EMBL:KPK20505.1, ECO:0000313|Proteomes:UP000051544};
RN [1] {ECO:0000313|EMBL:KPK20505.1, ECO:0000313|Proteomes:UP000051544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_41 {ECO:0000313|EMBL:KPK20505.1};
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:KPK20505.1}.
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DR EMBL; LJTT01000002; KPK20505.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8C9K9; -.
DR STRING; 1703391.AMJ67_00625; -.
DR PATRIC; fig|1703391.3.peg.3437; -.
DR Proteomes; UP000051544; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
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; 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 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; 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.
PE 4: Predicted;
FT DOMAIN 11..106
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
SQ SEQUENCE 707 AA; 73234 MW; FABF1599AE1F114D CRC64;
MARGVSSFER LFNPRGIAIV GASAEPARPG GQTIAALRQH GFKGGIYPVN PKYPEIAGHP
CCATVAEVRG ECDVAVIALP AAQVPGIIGA CGDRGIAFAV VLGGGFREAG ADGQKTEEAM
LSAARKGGVR IIGPNCLGLV NIPARVYAAW GSLTRPPLLP AGPVSAVLQS ASLGTTLLVR
CAAAGVGFRH VVTSGNETDV TAPELIEAYV DDAETRVILA YLEGVSDGHA LMRAARRALA
ARKPLIVLKA GNTEQGRRAA ASHTANLTGD YDVYRAVFRQ CGVIEVHDLD EAADVALCLV
GGRLPGGRRV AVMGGSGGAA AMFADRADEL RLSMPPLAEN TLNVLRRCLP PLSSLKNPID
YTAGYPRPVP GLDFQQAFDA VLADPGIDQL AVMFAAAGRN QLQVGGELLG KAASSSEKPI
VVFSGMSEEI APEGLGLMRA AGIPVLPSPK RAAVAMARLA DYSAALARRE HGSAAHGARS
VKAPALPPGA ATLDENESKK ILAAAGVPVT RDCFIAVDAM EGVPADIAFP VAVKIVSRDI
AHKTDIGAVR LNVRDGPALK AALSEILNNA RRAAPEARIA GALASEMITD GLETIIGVVN
DAVFGPVVVL GLGGILVETL GDASYRVAPF GLEDARAMIE ELRGRAVFDG VRGSAPRDID
ALVATLARVS ELAWHLRGRL LEMDINPLLV RSQGRGVVAA DALIVLR
//