ID A0A0P7WYB5_9RHOB Unreviewed; 666 AA.
AC A0A0P7WYB5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Acetyl-CoA synthetase {ECO:0000313|EMBL:KPQ06397.1};
DE EC=6.2.1.1 {ECO:0000313|EMBL:KPQ06397.1};
GN Name=acs-2 {ECO:0000313|EMBL:KPQ06397.1};
GN ORFNames=HLUCCA12_10425 {ECO:0000313|EMBL:KPQ06397.1};
OS Rhodobacteraceae bacterium HLUCCA12.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1666916 {ECO:0000313|EMBL:KPQ06397.1, ECO:0000313|Proteomes:UP000050476};
RN [1] {ECO:0000313|EMBL:KPQ06397.1, ECO:0000313|Proteomes:UP000050476}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLUCCA12 {ECO:0000313|EMBL:KPQ06397.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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:KPQ06397.1}.
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DR EMBL; LJSV01000009; KPQ06397.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7WYB5; -.
DR STRING; 1666916.HLUCCA12_10425; -.
DR PATRIC; fig|1666916.3.peg.164; -.
DR Proteomes; UP000050476; Unassembled WGS sequence.
DR GO; GO:0003987; F:acetate-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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 Ligase {ECO:0000313|EMBL:KPQ06397.1};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 7..97
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
SQ SEQUENCE 666 AA; 69146 MW; BB7B7250CA3F152A CRC64;
MRDLSRLLRP RSVAVLGSGW AANVVEQCQR MGYGGRVYPV HPTRSEIAGL PCFRALAELP
APPDATFIGV NRHATIDVVA ELAAMGAGGA VCFASGWRET GDDRLQDRLV AAAGAMPILG
PNCYGVINYL DGALLWPDQH GGRRVERGVA LISQSSNIVI NLTMQARGLP VAYVACLGNA
AQIGLTDLCA ALLADARVTA LGLYIEGLTD AAEFATLAEA ARAAGKGIVA LKSGKTEASR
GAAASHTASL AGGRAASSAY LRQAGVAEVD TPAELLETLK IVHQHGPGLG QRLCSLSCSG
GEAGLVADLA APFGLSLPAP DDAQRAGLSD LLGPLVSIAN PLDYHTFIWG DGPRTASVFA
TMLRGYDAGI FLIDPPRPDR CDPSSFEPAL DAIEAAARDT GIPAFPVASM PENFGEDRAI
ALMDRGIAPL MGLETALGAI RAAQAAPGRA GWRPWSPTAP HHALRLLAEP EAKARLAKAG
IAVPRGVHAA TLGALRPMVG VLTPPLALKG LGFAHKTEAG AVRLNLSSLE GQDEIPGATG
YLAEEMVTGA VAELLVGARR DPVYGATLTL GFGGVTAELL NDTATLVLPV TAQEVMQALR
GLRLWPLLDG YRGRARADAA AAVQVAMGLQ AMLQDDCMLE EIEINPLMVR ESGAVAVDAV
IWKEEP
//
