ID Q2K1H4_RHIEC Unreviewed; 684 AA.
AC Q2K1H4;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE SubName: Full=Probable acyl-CoA synthetase protein {ECO:0000313|EMBL:ABC93334.1};
GN OrderedLocusNames=RHE_PC00128 {ECO:0000313|EMBL:ABC93334.1};
OS Rhizobium etli (strain CFN 42 / ATCC 51251).
OG Plasmid p42c {ECO:0000313|EMBL:ABC93334.1,
OG ECO:0000313|Proteomes:UP000001936}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=347834 {ECO:0000313|EMBL:ABC93334.1, ECO:0000313|Proteomes:UP000001936};
RN [1] {ECO:0000313|EMBL:ABC93334.1, ECO:0000313|Proteomes:UP000001936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFN 42 / ATCC 51251 {ECO:0000313|Proteomes:UP000001936};
RX PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT seven interacting replicons.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
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DR EMBL; CP000136; ABC93334.1; -; Genomic_DNA.
DR RefSeq; WP_011427754.1; NC_007764.1.
DR AlphaFoldDB; Q2K1H4; -.
DR KEGG; ret:RHE_PC00128; -.
DR eggNOG; COG0045; Bacteria.
DR eggNOG; COG1042; Bacteria.
DR HOGENOM; CLU_007415_3_2_5; -.
DR OrthoDB; 9807426at2; -.
DR Proteomes; UP000001936; Plasmid p42c.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion 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; 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 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.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Plasmid {ECO:0000313|EMBL:ABC93334.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001936};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 485..684
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 684 AA; 72090 MW; 1905563358B9F735 CRC64;
MTSKPLDRLL RPQTIAVFGG REARRVIEQC DRMGFSGQIW PVHPKLEEVL GRPCYRSVSD
LPSAPDAAFV GVNRTLTVEI VRSLSDAGAG GAVCYASGFS EATAELADGT ELQQALMEAA
GDMPILGPNC YGLINGLDGA LLWPDQHGMK RIERGVAILT QSSNIALNLT MQTRGLPIAY
MVTAGNQAQT SLADIASALM EDQRVTAIGL HVEGFGDLAA LERLAAIARR LKKAVVVLKV
GRSEQAKHAA VSHTASLAGS DAVADAMLTR LGLGRVQSLP ALLETLKLLH IAGPLPSHSI
SSMSCSGGEA SLMADAAVGR EVEFPALQPQ QLPRLRQVLG DMVALSNPLD YHTFVWGDFE
RQAEAFRAMF EGGYALNLVV LDFPRGDRCD AAEWATTVDA VIAAASATGT LAGLLATLPE
NMPEPIADRL MANGIIAFSG IDEAIIAAEA AAGIGKVWDR PPPLPLLDVP SMDGEIETLT
EADAKTELAA CGLPVPWGLQ AFSPREAAEQ AERLGFPVVL KGLGIAHKTE AGAVVLNLRD
PEAVSNAAAA MPANGGYLIE KMIDPPVAEL IVGATRDPVF GLSLTLGAGG IFVELLDDSI
VLPLPATKAE IRDALLGLKI AKVIHGYRGR PRGDLDAAVD AVAAAAEYVV KNAVRLEELD
LNPLMVLPEG RGVVAVDALI RRRR
//
