ID A0A0S7ZRE8_9SPIR Unreviewed; 413 AA.
AC A0A0S7ZRE8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KPJ89656.1};
GN ORFNames=AMS17_00920 {ECO:0000313|EMBL:KPJ89656.1};
OS Spirochaetes bacterium DG_61.
OC Bacteria; Spirochaetota.
OX NCBI_TaxID=1704237 {ECO:0000313|EMBL:KPJ89656.1, ECO:0000313|Proteomes:UP000050987};
RN [1] {ECO:0000313|EMBL:KPJ89656.1, ECO:0000313|Proteomes:UP000050987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG_61 {ECO:0000313|EMBL:KPJ89656.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(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:KPJ89656.1}.
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DR EMBL; LJNB01000010; KPJ89656.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S7ZRE8; -.
DR Proteomes; UP000050987; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003878; F:ATP citrate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
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; 3.40.50.261; Succinyl-CoA synthetase domains; 1.
DR InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR032263; Citrate-bd.
DR InterPro; IPR005809; Succ_CoA_ligase-like_bsu.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR PANTHER; PTHR11815:SF10; SUCCINATE--COA LIGASE [ADP-FORMING] SUBUNIT BETA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11815; SUCCINYL-COA SYNTHETASE BETA CHAIN; 1.
DR Pfam; PF08442; ATP-grasp_2; 1.
DR Pfam; PF16114; Citrate_bind; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 1.
PE 4: Predicted;
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 17..194
FT /note="ATP-grasp fold succinyl-CoA synthetase-type"
FT /evidence="ECO:0000259|Pfam:PF08442"
FT DOMAIN 260..398
FT /note="ATP-citrate synthase citrate-binding"
FT /evidence="ECO:0000259|Pfam:PF16114"
SQ SEQUENCE 413 AA; 45442 MW; EF7A7F1153982078 CRC64;
MALRVTELTF LDFYAPRYGI PVPRHIWGTS EIEEIKRALE EWGGEAIVKP DVLSGERGKA
GSVVSVKNIH DALREIKRVS GVEVDGMMPR IAYLVEKISS KMEIYSAITY NSAFLAPSFT
LSLEGGIDVE DIQEENKVTI PIDIFRGLDA YQASQVLARL DCPKDLISTL SRCMVSFWDF
FISTGMEIAE INPWRVTPDG RPYACDFKGI VDEANYKAKV PGVEFPEYPE SFSDFEEEMR
GWDARSHQGQ AHVSDIGGTK ILPILFGGGI STIITETLES AGGRPMFLSD FGGNPPYERM
LGTAKICFAH RLAQAKLLLI LGGKANNTLI DVTFQAIADA LVSYAEEHGS ISTPVVIGRG
GPNLVKGLLA MKQALEYLKL PYIIFGPDTP VTMVAEYAAK LVNAFESIEE VEK
//
