ID U6MD66_9EIME Unreviewed; 517 AA.
AC U6MD66;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=succinate--CoA ligase (ADP-forming) {ECO:0000256|ARBA:ARBA00044045};
DE EC=6.2.1.5 {ECO:0000256|ARBA:ARBA00044045};
GN ORFNames=ENH_00006690 {ECO:0000313|EMBL:CDJ62157.1};
OS Eimeria necatrix.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=51315 {ECO:0000313|EMBL:CDJ62157.1};
RN [1] {ECO:0000313|EMBL:CDJ62157.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ62157.1};
RA Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA Tomley F., Pain A.;
RT "Genomic analysis of the causative agents of coccidiosis in chickens.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDJ62157.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ62157.1};
RA Aslett M.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + succinate = ADP + phosphate + succinyl-CoA;
CC Xref=Rhea:RHEA:17661, ChEBI:CHEBI:30031, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292,
CC ChEBI:CHEBI:456216; EC=6.2.1.5;
CC Evidence={ECO:0000256|ARBA:ARBA00043683};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
CC from succinyl-CoA (ligase route): step 1/1.
CC {ECO:0000256|ARBA:ARBA00005064}.
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DR EMBL; HG722368; CDJ62157.1; -; Genomic_DNA.
DR RefSeq; XP_013439519.1; XM_013584065.1.
DR AlphaFoldDB; U6MD66; -.
DR GeneID; 25470860; -.
DR VEuPathDB; ToxoDB:ENH_00006690; -.
DR OrthoDB; 1384037at2759; -.
DR UniPathway; UPA00223; UER00999.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
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; 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 SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:CDJ62157.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 53..278
FT /note="ATP-grasp fold succinyl-CoA synthetase-type"
FT /evidence="ECO:0000259|Pfam:PF08442"
FT DOMAIN 376..478
FT /note="ATP-citrate synthase/succinyl-CoA ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00549"
FT REGION 282..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 79..106
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 282..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 517 AA; 55867 MW; 5FB40A52732585DE CRC64;
MQLLARLAVG RGGPLQRWGA PAAGILGQQQ LLQQPLQQQQ QQLQQLQQRR HLNLYEYQSM
QLLQQHNVAV PRFRIARTPE EAQAAAAALQ QELQQQQQQQ QQQQQQQQPG LVVKAQVLAG
GRGLGYFKEN GYKGGVQRCS SPQQVFAAAA NMLQQTLITK QTGAAGKVCS TILICEEFKA
KRELYLAIIL DRNTGVPMLI ASSQGGTSIE DIAHSNPEAI KKIRMGFDEA LGADALEELR
IHLNLSPAMG RQLDSLISSL HKLFISRDCL LVEINPLILT DKPPQQQQQQ QQQQQQQQQE
PQQELWAADA KLSVDDNAKY RQLDLFESVA AEEKAAQQQC AAAAAGGAAA AAAALEAAAE
QQQLQYVKLG AGVGCLVNGA GLAMATMDLL QLQGGAAANF LDLGGAAAAP QIALALQLLR
SDAAAPVLFL NIFAGILKCD EIAKGLVQAA RQHKIHKPIV VRLQGTNKEK AEAILKEAME
GPEGASLHIE AINDFEAAAT RAVQLAKELL QQQQAAQ
//
