ID A1RXJ2_THEPD Unreviewed; 372 AA.
AC A1RXJ2;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Succinyl-CoA synthetase (ADP-forming) beta subunit {ECO:0000313|EMBL:ABL77922.1};
DE EC=6.2.1.5 {ECO:0000313|EMBL:ABL77922.1};
GN OrderedLocusNames=Tpen_0516 {ECO:0000313|EMBL:ABL77922.1};
OS Thermofilum pendens (strain DSM 2475 / Hrk 5).
OC Archaea; Thermoproteota; Thermoprotei; Thermofilales; Thermofilaceae;
OC Thermofilum.
OX NCBI_TaxID=368408 {ECO:0000313|EMBL:ABL77922.1, ECO:0000313|Proteomes:UP000000641};
RN [1] {ECO:0000313|Proteomes:UP000000641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2475 / Hrk 5 {ECO:0000313|Proteomes:UP000000641};
RX PubMed=18263724; DOI=10.1128/JB.01949-07;
RA Anderson I., Rodriguez J., Susanti D., Porat I., Reich C., Ulrich L.E.,
RA Elkins J.G., Mavromatis K., Lykidis A., Kim E., Thompson L.S., Nolan M.,
RA Land M., Copeland A., Lapidus A., Lucas S., Detter C., Zhulin I.B.,
RA Olsen G.J., Whitman W., Mukhopadhyay B., Bristow J., Kyrpides N.;
RT "Genome sequence of Thermofilum pendens reveals an exceptional loss of
RT biosynthetic pathways without genome reduction.";
RL J. Bacteriol. 190:2957-2965(2008).
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DR EMBL; CP000505; ABL77922.1; -; Genomic_DNA.
DR AlphaFoldDB; A1RXJ2; -.
DR STRING; 368408.Tpen_0516; -.
DR EnsemblBacteria; ABL77922; ABL77922; Tpen_0516.
DR KEGG; tpe:Tpen_0516; -.
DR eggNOG; arCOG01337; Archaea.
DR HOGENOM; CLU_037430_0_2_2; -.
DR OrthoDB; 146449at2157; -.
DR Proteomes; UP000000641; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) 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; IPR017866; Succ-CoA_synthase_bsu_CS.
DR InterPro; IPR005811; SUCC_ACL_C.
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; PF00549; Ligase_CoA; 1.
DR PIRSF; PIRSF001554; SucCS_beta; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 1.
DR PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1.
PE 4: Predicted;
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ABL77922.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000000641}.
FT DOMAIN 4..192
FT /note="ATP-grasp fold succinyl-CoA synthetase-type"
FT /evidence="ECO:0000259|Pfam:PF08442"
FT DOMAIN 254..368
FT /note="ATP-citrate synthase/succinyl-CoA ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00549"
SQ SEQUENCE 372 AA; 40795 MW; B7E6D540FEAA909B CRC64;
MIPYEFEVKD IFEKFQVPVE KSCLLTHEAL KDSLGCIKGL RTPLIVKAQV RGWGRGKAGL
VKSAENPEEA LKVAQEFFLR EFNGEKIRYV LVSERKRILR EMYLSFMVSS NPPGFLLLAS
KHGGVDVEEL SKTPGGLLKI FIDPFEGLRD YMVRTVAGYL GVPQEHIEKI LRSLWQIFRE
YNFTLLEVNP LALTEDGVLA LDRKGVIDDD ASRKSSLTGI FARYFSELDE LSLSAFQKGF
SVVKLDGDTA VVGNGAGLTM ATLDAVLEAG ARPGLFLDLG GGADAERVRE ALLLVLKQQN
ISKILLNILG GITRCDEVAR GVVQALSSAK PSSVKVAVRL SGFMEDEGRR ILREAGLSAF
DSLEEAVASL LG
//
