ID A0A0B4CYZ5_9RHOB Unreviewed; 663 AA.
AC A0A0B4CYZ5;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Acyl-CoA synthetase {ECO:0000313|EMBL:KIC46241.1};
GN ORFNames=RA29_19735 {ECO:0000313|EMBL:KIC46241.1};
OS Tateyamaria sp. ANG-S1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Tateyamaria.
OX NCBI_TaxID=1577905 {ECO:0000313|EMBL:KIC46241.1, ECO:0000313|Proteomes:UP000031171};
RN [1] {ECO:0000313|Proteomes:UP000031171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANG-S1 {ECO:0000313|Proteomes:UP000031171};
RX PubMed=25755651; DOI=10.3389/fmicb.2015.00123;
RA Collins A.J., Fullmer M.S., Gogarten J.P., Nyholm S.V.;
RT "Comparative genomics of Roseobacter clade bacteria isolated from the
RT accessory nidamental gland of Euprymna scolopes.";
RL Front. Microbiol. 6:123-123(2015).
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:KIC46241.1}.
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DR EMBL; JWLL01000015; KIC46241.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B4CYZ5; -.
DR STRING; 1577905.RA29_19735; -.
DR Proteomes; UP000031171; 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:UP000031171};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 1..92
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
SQ SEQUENCE 663 AA; 68635 MW; F3B589E41AB1ACEB CRC64;
MLRPKSIAVI GGGAWCVSVI EQAERFGFDG AIWPVHPTKA MVGGHGAFPS VADLPDAPDA
AFVGVNRAAT IGVVEDLSRI GTGGAVCFAS GFSEAGAEDT DAASLQDQLV AAAGDMPILG
PNCYGFINAL DQALLWPDQH GCAPVDRGVA ILTQSSNIAI NLTMQQRALP IAYVITCGNM
AQTSQAELAL ALLDDPRVTA IGLHVEGFGS LRGWEALAAL AHERGVPLVA LKVGASDRAR
QATISHTASL AGSDSGAQAF LNRLGIARVA NLPDFLETLK LLHLNGPISG NGIASISCSG
GEASLIADMA VGTGLTFPSL SHGQRASLRD ALGPMVSLAN PLDYHTYIWR DAPRMAQAWA
AMTGEEIGMT LSIVDYPATD ATDWTCTVDA AIAAKAMTGA PFGVVATLPE LMPPETAEHL
AANGVVPFHG LREALAAVDA VQSIEPPHKD PICLPGTASA DTVLLEAEAK AALAAYGIDV
PWNVATAPEN MADTLPSLSG PFAVKGIGIA HKTEANAVRL NVAREDILST AKDIGTPTVL
IEEMVTDDVA EMLIGVVRDP AHGFVLTIGA GGVLTELVQD TVHLLLPVRA TDVQAALYRL
RCSALLDGYR GKPAANVAAV IDAVLAIQNY VLAHSDTVSE VEVNPLICTP TRAVAVDALI
RKA
//
