ID Q5P044_AROAE Unreviewed; 712 AA.
AC Q5P044;
DT 04-JAN-2005, integrated into UniProtKB/TrEMBL.
DT 04-JAN-2005, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE SubName: Full=Organic acid-CoA ligase (ADP forming),similar to feruloyl-CoA synthetase {ECO:0000313|EMBL:CAI09320.1};
GN Name=ferA {ECO:0000313|EMBL:CAI09320.1};
GN ORFNames=ebA5611 {ECO:0000313|EMBL:CAI09320.1};
OS Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Aromatoleum.
OX NCBI_TaxID=76114 {ECO:0000313|EMBL:CAI09320.1, ECO:0000313|Proteomes:UP000006552};
RN [1] {ECO:0000313|EMBL:CAI09320.1, ECO:0000313|Proteomes:UP000006552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EbN1 {ECO:0000313|EMBL:CAI09320.1,
RC ECO:0000313|Proteomes:UP000006552};
RX PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA Reinhardt R.;
RT "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT bacterium, strain EbN1.";
RL Arch. Microbiol. 183:27-36(2005).
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DR EMBL; CR555306; CAI09320.1; -; Genomic_DNA.
DR RefSeq; WP_011238986.1; NC_006513.1.
DR AlphaFoldDB; Q5P044; -.
DR STRING; 76114.ebA5611; -.
DR KEGG; eba:ebA5611; -.
DR eggNOG; COG0045; Bacteria.
DR eggNOG; COG1042; Bacteria.
DR HOGENOM; CLU_007415_3_1_4; -.
DR OrthoDB; 8664175at2; -.
DR Proteomes; UP000006552; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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; 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.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Ligase {ECO:0000313|EMBL:CAI09320.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000006552}.
FT DOMAIN 500..537
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 712 AA; 74308 MW; E20C4988616A86EB CRC64;
MNHPSPALVA RLLQPASIAI IGVSADARSL GGVVLGNLER FGYRGDIHLV SRNSPEVNGR
ACVQTVDQLP HGIDVAVLTV PEAAVLGTVQ ACGARGVGAV VVFASGYAEA GPEGEARQEA
LAAAARAAGI ALAGPNCMGL TNFRAGIPLT FESIEPYPSS DVPGVSIVAQ SGAMANNIRE
AMIGRGLPIT HSVSTGNEAV LSLEDYVEYF IADVNTCVIA VYAEQVRQPL RFLELAGRAR
AAGKPIVLTM IGRSERAREA AQSHTGALTG DYATASALLG AEAVIVATTL DELFDVIPLL
LRHPQPSAAG LAFVTGSGAM KNVALDLGQD LGLEFPAFTH GTVEKLQTIL PGYAVSENPL
DYTTVSMRDP ALMGTVIDVV VADPNCGGVI VAQMAGSALG QRDKAEHMVP AVARADKPAA
LVIMGDDGPL HPVLADAVRT SGVPFFRSPD RAMRAMALVN RYGLALEQRR EAAAPAVLPA
LSHPPSAFPE GGVIAEYRGK AWLAQAGLPT PPGALARDVD EAVRIATGLG WPVVLKAQAS
ALPHKSDVGG VIVNIGDEAG LRAAWTRMQD DVARARPDLV LDGILVEKMG ARGLELVVGA
RRDPQWGPIV LVGLGGIWIE VLKDVRLLPA DADEAHIVRE LGKLKAAAML DGLRGQPPVD
KRALARAVAT VGALMRTMPE IREIDINPLV AYPGSVLALD ALIVCESKDD RR
//
