ID S9Q9I8_9RHOB Unreviewed; 705 AA.
AC S9Q9I8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Acetyl-CoA synthetase {ECO:0000313|EMBL:EPX76627.1};
GN ORFNames=Salmuc_00459 {ECO:0000313|EMBL:EPX76627.1};
OS Salipiger mucosus DSM 16094.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Salipiger.
OX NCBI_TaxID=1123237 {ECO:0000313|EMBL:EPX76627.1, ECO:0000313|Proteomes:UP000015347};
RN [1] {ECO:0000313|Proteomes:UP000015347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16094 {ECO:0000313|Proteomes:UP000015347};
RX PubMed=25197501; DOI=10.4056/sigs.4909790;
RA Riedel T., Spring S., Fiebig A., Petersen J., Kyrpides N.C., Goker M.,
RA Klenk H.P.;
RT "Genome sequence of the exopolysaccharide-producing Salipiger mucosus type
RT strain (DSM 16094(T)), a moderately halophilic member of the Roseobacter
RT clade.";
RL Stand. Genomic Sci. 9:1331-1343(2014).
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:EPX76627.1}.
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DR EMBL; APVH01000046; EPX76627.1; -; Genomic_DNA.
DR RefSeq; WP_020039345.1; NZ_KE557282.1.
DR AlphaFoldDB; S9Q9I8; -.
DR STRING; 1123237.Salmuc_00459; -.
DR eggNOG; COG1042; Bacteria.
DR HOGENOM; CLU_007415_3_1_5; -.
DR Proteomes; UP000015347; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
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;
KW Reference proteome {ECO:0000313|Proteomes:UP000015347};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 17..112
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
SQ SEQUENCE 705 AA; 72043 MW; FC6B741413F93295 CRC64;
MTRAADVLGD GSLARALFAP RAVALIGASS DPGKTTARPL RYLRKHGFEG RVFPIHPTAA
TVGGTTAYPD LASVPEPVDH AFILLAAPLV PAAVRACAEA GVRCVTVLSD GFAETGPEGL
ARQRALVETA RAHGVRLLGP NSIGVVDTDG FACSANAALE MPELPRAGYG VISQSGSMIG
ALLSQGAARG IGFSSLVSVG NECDLSVGEI GELMLADPRC TAILLFLEAI RDRAALARFA
RAAEAAGKPV LACKLGRSTA GQALAATHTG ALSGDDRSAE ALFRHLGIAR VNMLETLYEA
PPLFFGSGRP EGGRVAVVTT TGGGGALVVD ALASNGLDIA AVPATVRARL ERQGVSVGQS
GLIDLTLAGT GPEVVRDVLD LLMAAEGVDA VAMVIGSSAQ FRPDLAVAPL HGLAESPKPL
AIHLVPAAER SRAMLSAEGL AVFRTAESCA EGLRARLQRR APGDVPATPA EGLAERVAAE
VAGAAGAALD EPTSRRICDL LGIEGPPGRC VRTPDEARAA FAELGGAAVL KIVSPDIPHK
SDSGGILLGI DTPEAAARGV AQLLQTQRAA HPGADLRGVL IQKMARGVGE ALIGFRRDPQ
SGPFVMLGAG GVLAEVMDDI AIRVAPVDLD TAREMIAEVR MFRAFAGYRG APKGDLEAVA
RAVVSLSRLA RCPEVAEAEI NPFLIGAEGA GGLALDALVV AAERP
//
