ID B4D2X3_9BACT Unreviewed; 902 AA.
AC B4D2X3;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE SubName: Full=CoA-binding domain protein {ECO:0000313|EMBL:EDY19084.1};
GN ORFNames=CfE428DRAFT_3261 {ECO:0000313|EMBL:EDY19084.1};
OS Chthoniobacter flavus Ellin428.
OC Bacteria; Verrucomicrobiota; Spartobacteria; Chthoniobacterales;
OC Chthoniobacteraceae; Chthoniobacter.
OX NCBI_TaxID=497964 {ECO:0000313|EMBL:EDY19084.1, ECO:0000313|Proteomes:UP000005824};
RN [1] {ECO:0000313|EMBL:EDY19084.1, ECO:0000313|Proteomes:UP000005824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ellin428 {ECO:0000313|EMBL:EDY19084.1,
RC ECO:0000313|Proteomes:UP000005824};
RX PubMed=21460085; DOI=10.1128/JB.00295-11;
RA Kant R., van Passel M.W., Palva A., Lucas S., Lapidus A.,
RA Glavina Del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S.,
RA Larimer F.W., Land M.L., Hauser L., Sangwan P., de Vos W.M., Janssen P.H.,
RA Smidt H.;
RT "Genome sequence of Chthoniobacter flavus Ellin428, an aerobic
RT heterotrophic soil bacterium.";
RL J. Bacteriol. 193:2902-2903(2011).
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:EDY19084.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ABVL01000009; EDY19084.1; -; Genomic_DNA.
DR AlphaFoldDB; B4D2X3; -.
DR STRING; 497964.CfE428DRAFT_3261; -.
DR eggNOG; COG1042; Bacteria.
DR eggNOG; COG1670; Bacteria.
DR InParanoid; B4D2X3; -.
DR Proteomes; UP000005824; Unassembled WGS sequence.
DR GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:InterPro.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.40.630.30; -; 1.
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; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR003781; CoA-bd.
DR InterPro; IPR000182; GNAT_dom.
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; PF13302; Acetyltransf_3; 1.
DR Pfam; PF13549; ATP-grasp_5; 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; SSF55729; Acyl-CoA N-acyltransferases (Nat); 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.
DR PROSITE; PS51186; GNAT; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000005824}.
FT DOMAIN 505..541
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 745..902
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 902 AA; 96655 MW; 0F70526A853112BC CRC64;
MKARTARPSL SARRIPLSEI LNPQSIAVIG ATEAEHSVGR AILENLSAFQ GRVFAVNPKH
KTVLGVPAFA SIGAIPEPID LAIVATPAST VPAILGECAA AGVKGAVIIS AGFKETGASG
AELERQILAQ RGHMRVLGPN CLGVMLPHIG LNATFAASMA RAGKVAFLSQ SGALCTAILD
WSLREEVGFS AFVSLGSMLD IGWGDLIEFF GDDPQTKSIV CYMESVGDAR TFLSAAREVA
FSKPIVVIKV GRTEAAARAA ASHTGSLTGS DAVLDAAFRR AGVVRVETIE ELFDIAEVLA
KQPPPRGPRL AIVTNAGGPG ALATDILVTA GGQLAKLSPQ TLTKLDQLLP PAWSHGNPID
LLGAADAETY GRAFEIALSE ESVDGVLVIL TPQAMTDIDG TATQLANLAR GSSKPVLASW
MGGASLESAR TALNAAGVPT YDYPDAAART FALMWQYSDR LRLLYERPAL PPADSSKGEK
HSIAERLIAH ARKEGRNLLT EVESKHLLSA YGIPTVETFI AHTENAAVNR AQRLGYPVVV
KVYSQTITHK TDVGGVRLQL ENGAAVRRAW REIKEAVSAK AGADQFQGVT VQSMIPRDGV
ELIFGASVDP QFGPVLIFGA GGELVEVLKD RAIGLPPLTT TLARRLMERT RIFHALKGVR
GRKPVNLDAL AELLVAFSHL VAEQPWIAEI DINPLLASAE HLLALDARVV LHPINKAESD
LPHLAIRPYP TDYVSQIRLR QGSRLTLRPI RPDDEELLVA FHATLSEESV SFRYFGPLSL
ETRTAHHRLV RVCFSDYDRE LALVTVHGKG AEREIVAVGR LNRLHGTNSA EFAILVADTW
QGRGLGTQLL EALVRIGKSE KLELIVGSIL ANNHAMLDLS RRLGFELKRL PGENVVEAEL
RL
//
