GenomeNet

Database: UniProt
Entry: A0A0H4LE96_9RHOB
LinkDB: A0A0H4LE96_9RHOB
Original site: A0A0H4LE96_9RHOB 
ID   A0A0H4LE96_9RHOB        Unreviewed;       699 AA.
AC   A0A0H4LE96;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   28-MAR-2018, entry version 13.
DE   SubName: Full=Acyl-CoA synthetase (NDP forming) {ECO:0000313|EMBL:AKO98928.1};
GN   ORFNames=MALG_03791 {ECO:0000313|EMBL:AKO98928.1};
OS   Marinovum algicola DG 898.
OG   Plasmid pMaD1 {ECO:0000313|EMBL:AKO98928.1,
OG   ECO:0000313|Proteomes:UP000036352}.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Marinovum.
OX   NCBI_TaxID=988812 {ECO:0000313|EMBL:AKO98928.1, ECO:0000313|Proteomes:UP000036352};
RN   [1] {ECO:0000313|EMBL:AKO98928.1, ECO:0000313|Proteomes:UP000036352}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DG 898 {ECO:0000313|EMBL:AKO98928.1,
RC   ECO:0000313|Proteomes:UP000036352};
RC   PLASMID=Plasmid pMaD1 {ECO:0000313|Proteomes:UP000036352};
RX   PubMed=26079637; DOI=10.1111/1462-2920.12947;
RA   Frank O., Goker M., Pradella S., Petersen J.;
RT   "Ocean's twelve: Flagellar and biofilm chromids in the multipartite
RT   genome of Marinovum algicola DG898 exemplify functional
RT   compartmentalization.";
RL   Environ. Microbiol. 17:4019-4034(2015).
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; CP010856; AKO98928.1; -; Genomic_DNA.
DR   RefSeq; WP_043752987.1; NZ_CP010856.1.
DR   EnsemblBacteria; AKO98928; AKO98928; MALG_03791.
DR   KEGG; malg:MALG_03791; -.
DR   PATRIC; fig|988812.14.peg.3800; -.
DR   Proteomes; UP000036352; Plasmid pMaD1.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0048037; F:cofactor binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.40.50.261; -; 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   Pfam; PF13380; CoA_binding_2; 1.
DR   Pfam; PF13607; Succ_CoA_lig; 1.
DR   SMART; SM00881; CoA_binding; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF52210; SSF52210; 2.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Complete proteome {ECO:0000313|Proteomes:UP000036352};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Plasmid {ECO:0000313|EMBL:AKO98928.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036352}.
FT   DOMAIN      485    522       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   699 AA;  72116 MW;  2254A816A6A218EA CRC64;
     MVARDFPDLS RLLSPRSVAI LGASERPRSV GSDTLLNLAE HSDFDGQIFP VNPGRERVHG
     LRAYSAMSAL PGPVDVAVVC LPADAVVGAL RDCAAAGTGF AVVFTSGFGE TGDEGRAVEA
     EMAEIARQSG MRIYGPNSPG LSNINRRLGL TFSPVFKNDT LSGGIGLVTQ GGGLGRAFIQ
     ASERGIGVGL WCSTGNEADL TMADVVYHMV GDPDIKVIAL LAEGFRDGPR FLAAARAAAR
     AGKPVVAMKV GKSDYGVAAT RSHTAALAGS AAVTSALFRQ HGIVEVEDLD ELIDTAALFE
     RAGIAPRRGI CVYSFSGGTA ALAADMVGSA GLILSELAPG TRAGLRALAP SYAAVDNPVD
     LTTQVFTQDK LNRDCLSLVA RDPATDVVLL PIPADYGPIT DRSADDMVAL APDSPALLLP
     VWMSGHRAAG YATLNAAGLA PFRSLGKAVT ALKRLIWRGD WSPSGTSTLA LPAFPPGELD
     EAAAKAVLAD LGLTVPEGRV VTSARQAGEA ARGIGFPVVL KALVPGLLHK TEAGAVAVGL
     MDEQALAAAW GAMMTSLSAQ GHRLERALVE RMEHGPGVEV MAGLHRDPVF GPVVSFGLGG
     VMVEALSDVT HRAAPFGRDE ALAMIDEIRG RALLGPLRGR PGADLGALAD LLVILAALGA
     RGDIAEMDLN PVRAGPAGAT VLDAVILRAP TEIEGKARQ
//
DBGET integrated database retrieval system