ID A8TIY2_9PROT Unreviewed; 704 AA.
AC A8TIY2;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Putative pimeloyl-CoA synthetase {ECO:0000313|EMBL:EDP66605.1};
GN ORFNames=BAL199_16128 {ECO:0000313|EMBL:EDP66605.1};
OS alpha proteobacterium BAL199.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=331869 {ECO:0000313|EMBL:EDP66605.1, ECO:0000313|Proteomes:UP000003417};
RN [1] {ECO:0000313|EMBL:EDP66605.1, ECO:0000313|Proteomes:UP000003417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAL199 {ECO:0000313|EMBL:EDP66605.1,
RC ECO:0000313|Proteomes:UP000003417};
RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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:EDP66605.1}.
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DR EMBL; ABHC01000001; EDP66605.1; -; Genomic_DNA.
DR AlphaFoldDB; A8TIY2; -.
DR STRING; 331869.BAL199_16128; -.
DR eggNOG; COG1042; Bacteria.
DR OrthoDB; 9807426at2; -.
DR Proteomes; UP000003417; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000003417};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 494..530
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 704 AA; 72474 MW; 1BC485965CE3F950 CRC64;
MTRDVSSLIR PATIAVIGAS ATKRAQGNAV IDNLLSRDCG RRIIPVHRSA GTVQGLATVA
TIEDLPDGVD LAIASVPAGA AAETARALEA RGVKSAIFFA SGFSPADGEA FRSLAAASAM
NIQGPNCMGL INLNDALFLY PATTSSKIRA GKVAFVAQSG SAAITLMNSA EFGISKIITV
GSEFQLTAAD YMDWLATDDD TAAIGVVLEA IKDPDAFARA ARRIRDNGKS LTILKVGNSE
VGSAATLAHT GSMTNDADTY RLYFEANGIA TVDDYDELNA SLEILSRHGQ RHGTGRLAIV
GISGGQTALA CDVAAAAGIE LARFGDAVVR DMGRVSPGTL AQNPIDFGSV VDEAARDIAG
SIKAVLDDDG IDVLAVIQDC QAGLHPKSLE SYTTPIDAYC RSAVAASKPI VAISPTSEEI
HPGVRATFES HGIPIVSGLR EGLVGIRTIS RPHPRPPADT PETPGTLARK TRALGLIQDG
LKSGRSQLAP DACMEILAAY GIPTPPSLVV GNASEAVARV AEVGFPLAVK IASKDIAHRS
ELGGVVLGVN DVDGLSAAIA RIAGSVAAAA PDAAIDGYEL QREVRGDLEA VVGFVASPPF
GVKVMVGTGG TLVELTGDLA MGLAPLTVAD AQALIASTKL GQRLDGYRNL IARTDTRPLA
ELVANLSLMA RELGDRITGC DLNPVMIRAG SGDVVVVDVL MTVG
//
