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Database: UniProt
Entry: A0A0S8C9K9_9PROT
LinkDB: A0A0S8C9K9_9PROT
Original site: A0A0S8C9K9_9PROT 
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
//
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