ID A6LCX9_PARD8 Unreviewed; 686 AA.
AC A6LCX9;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=Acetyl-CoA synthetase {ECO:0000313|EMBL:ABR43543.1};
GN OrderedLocusNames=BDI_1804 {ECO:0000313|EMBL:ABR43543.1};
OS Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM
OS 5825 / NCTC 11152).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Parabacteroides.
OX NCBI_TaxID=435591 {ECO:0000313|EMBL:ABR43543.1, ECO:0000313|Proteomes:UP000000566};
RN [1] {ECO:0000313|EMBL:ABR43543.1, ECO:0000313|Proteomes:UP000000566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152
RC {ECO:0000313|Proteomes:UP000000566};
RX PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA Knight R.D., Gordon J.I.;
RT "Evolution of symbiotic bacteria in the distal human intestine.";
RL PLoS Biol. 5:1574-1586(2007).
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DR EMBL; CP000140; ABR43543.1; -; Genomic_DNA.
DR RefSeq; WP_005855031.1; NZ_LR215978.1.
DR AlphaFoldDB; A6LCX9; -.
DR STRING; 435591.BDI_1804; -.
DR PaxDb; 435591-BDI_1804; -.
DR GeneID; 57234683; -.
DR KEGG; pdi:BDI_1804; -.
DR eggNOG; COG0045; Bacteria.
DR eggNOG; COG1042; Bacteria.
DR HOGENOM; CLU_007415_3_1_10; -.
DR BioCyc; PDIS435591:G1G5A-1856-MONOMER; -.
DR Proteomes; UP000000566; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
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:UP000000566}.
FT DOMAIN 6..101
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
SQ SEQUENCE 686 AA; 74743 MW; 4A62853927935BDB CRC64;
MINRELINPQ SIVVVGGSNN VHKPGGRIVR NLLDGKYKGE LCVVNAKETD VQGVKSYPSV
HDIPETELAI ISIPSKSCPE VMEVLARQKG VKAFIVISAG FGEETHEGGI LEQQMLDVVN
EAGASLIGPN CIGLMNMNYH GVFTQPIPEF HPDGVDFISS SGGTALFIIE SALTKGLRFS
SVWSVGNSKQ NGVEDILEYM DRNFDPVLDS KIKMLYIEQI KQPDKLLYHA SSLIRKGCKI
AAIKAGSTES GKRAASSHTG AIASSDSAVE ALFRKAGIVR CFSREELTTV ASIFTLKDVK
GKNCAIVTHA GGPAVMLADA LSKGRLNVPS LEGPIADELK SKLYPGAAVG NPIDIIGTGT
PEHLATAIDF CENRFDNVDL MMVIFGSPGL VKLYDTYEVL HKKMEECKKP IFPILPSIVT
AGPEVKSFVK KGHVNFSDEV TLGTALSRVI NTPKPMSTDI QLYGVDVPEV RRIIDRLPGS
GYLNPEEVRT LLRAANIPLV EEYASDDRDA LLAFAKKVKY PVVAKVVGPV HKSDIGGVAL
NIRGEEHLLF EYERMMRLPG VTGIMVQPML KGQELFLGAK YEDRFGHVVL CGLGGIFVEV
LKDVSYGLAP LSYDETYSMI RSLRGYPIIK GTRGQKGIDE QQYADIIVRL STLLRFASEI
KEMDINPLVA TDRGLFAVDA RIRIEK
//
