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Database: UniProt
Entry: Q5LPZ9_RUEPO
LinkDB: Q5LPZ9_RUEPO
Original site: Q5LPZ9_RUEPO 
ID   Q5LPZ9_RUEPO            Unreviewed;       697 AA.
AC   Q5LPZ9;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   SubName: Full=Acyl-CoA synthetase, putative {ECO:0000313|EMBL:AAV95942.1};
GN   OrderedLocusNames=SPO2697 {ECO:0000313|EMBL:AAV95942.1};
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter
OS   pomeroyi).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200 {ECO:0000313|EMBL:AAV95942.1, ECO:0000313|Proteomes:UP000001023};
RN   [1] {ECO:0000313|EMBL:AAV95942.1, ECO:0000313|Proteomes:UP000001023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M.,
RA   Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q.,
RA   Daugherty S.C., Deboy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA   Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine
RT   environment.";
RL   Nature 432:910-913(2004).
RN   [2] {ECO:0000313|EMBL:AAV95942.1, ECO:0000313|Proteomes:UP000001023}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
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DR   EMBL; CP000031; AAV95942.1; -; Genomic_DNA.
DR   RefSeq; WP_011048399.1; NC_003911.12.
DR   AlphaFoldDB; Q5LPZ9; -.
DR   STRING; 246200.SPO2697; -.
DR   PaxDb; 246200-SPO2697; -.
DR   KEGG; sil:SPO2697; -.
DR   eggNOG; COG0045; Bacteria.
DR   eggNOG; COG1042; Bacteria.
DR   HOGENOM; CLU_007415_3_2_5; -.
DR   OrthoDB; 9807426at2; -.
DR   Proteomes; UP000001023; Chromosome.
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:UP000001023};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          12..102
FT                   /note="CoA-binding"
FT                   /evidence="ECO:0000259|SMART:SM00881"
SQ   SEQUENCE   697 AA;  73358 MW;  432F82A3FE4A0ED3 CRC64;
     MRPAQRENFR RLLTPRHIAF VGGRDAAIAI REARRRGFAG RMWAVNPKRD VLEGVACVPT
     IADLPEAPDA VYLAIPAAAV TGALGQLSAM GVGGVVCFSA GFKETGDAAA ERALIAAAGD
     MALIGPNCYG LINYVGNSAL WSFEHGGWSP GYGAAIITQS GMFSSDITMS QRSLPMAYMV
     SAGNQAVLGL EDFLDAFASD PVVRAIGLHI EGLQDVARFE RTALRALERG VPVVALKSGS
     SRIGAALTIS HTGSLSGANE LYEALFARCG VISVSNPSQF LETLKLLCVT GAPRGARVAG
     FTCSGGGATM LADHAERIGL SFPAVEGAHR TELKALLPEI ATVSNPLDYT TPIWGQGEHT
     YPVFSRTLEA VTPDFTVLVQ DYPAAGLDES KVFYLNDAGA FARAATEQQV PAAILATIPE
     NMDAETRQML IEQGVAPMQG IHEALNAIRD AAGWSAARAR ILSAKPAPLL PPLVPANLVG
     QTEDIGKDWL RGAGCAVPEG RSVTAREVES AAAEIGFPVA LKMMSPRLAH KTEAGAVALN
     VADQSELRAA LAQMPGAVAA YDPDALTDRF LVEAMSPPPL AELILTLRRD PQFGHALVLG
     SGGVLVELLG DAVTLLLPCS VADVQRGLEG LRLAPLLGGY RGRPAADLAR IADDIYALTR
     AYLQDCAEIA EVEINPLFVY PDRVVAIDVL LHRVAGQ
//
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