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Database: UniProt
Entry: A0A061QFK7_9PROT
LinkDB: A0A061QFK7_9PROT
Original site: A0A061QFK7_9PROT 
ID   A0A061QFK7_9PROT        Unreviewed;       464 AA.
AC   A0A061QFK7;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=CoA-binding domain-containing protein {ECO:0000259|SMART:SM00881};
GN   ORFNames=AQ1_02199 {ECO:0000313|EMBL:GAK34301.1};
OS   alpha proteobacterium Q-1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria.
OX   NCBI_TaxID=1492281 {ECO:0000313|EMBL:GAK34301.1, ECO:0000313|Proteomes:UP000027360};
RN   [1] {ECO:0000313|EMBL:GAK34301.1, ECO:0000313|Proteomes:UP000027360}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Q-1 {ECO:0000313|EMBL:GAK34301.1,
RC   ECO:0000313|Proteomes:UP000027360};
RX   PubMed=22447601; DOI=10.1128/AEM.00084-12;
RA   Suzuki M., Eda Y., Ohsawa S., Kanesaki Y., Yoshikawa H., Tanaka K.,
RA   Muramatsu Y., Yoshikawa J., Sato I., Fujii T., Amachi S.;
RT   "Iodide oxidation by a novel multicopper oxidase from the
RT   alphaproteobacterium strain Q-1.";
RL   Appl. Environ. Microbiol. 78:3941-3949(2012).
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:GAK34301.1}.
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DR   EMBL; BAYV01000028; GAK34301.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A061QFK7; -.
DR   STRING; 1492281.AQ1_02199; -.
DR   OrthoDB; 9807426at2; -.
DR   Proteomes; UP000027360; Unassembled WGS sequence.
DR   GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
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; 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; 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; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 2.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000027360};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          13..108
FT                   /note="CoA-binding"
FT                   /evidence="ECO:0000259|SMART:SM00881"
SQ   SEQUENCE   464 AA;  48475 MW;  75CC9B17723A1C46 CRC64;
     MSTAQAGRDL SAFFAPRSVA IVGASARPTS SGGAILHMME EAGFAGALYP INPKGGEMYG
     RQALPDLRAL PSPVDLVVIA IRPDFILDAV TEAADTGHKA ILILPGGFAE AGDEGAERQA
     ALDALAEKHD LIIAGPNCGG IISLGDQTRL AATFFRDLPP GGPIAFISQS GALAEEMIAH
     AVACRVPLGR VVSVGNSMHL GVEDHLRHLG DDPETGAILL YLESARDMAS LAATARSVSC
     SKPIVALIPG RTQKGLDAAK AHTGASASSD AAIDALCRDA GIVRVKSLRD LQLAARGLGF
     FPKGFGKRAL ILSNSGGPGV LTTDEATLSG LDLVDLPAPM AAALKDALPK EASVRNPLDL
     LADAREDRFG ETLAIAMAHR AAFDVILMIH VVPFMVDADP VIARLAEKAA ACDLPLMHSM
     MGTLEQRDRW FANMEQAGVP MFSNSEDMAR TAGILAQCYS VRDH
//
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