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Database: UniProt
Entry: D7EYH9_9EUKA
LinkDB: D7EYH9_9EUKA
Original site: D7EYH9_9EUKA 
ID   D7EYH9_9EUKA            Unreviewed;       307 AA.
AC   D7EYH9;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Scs alpha {ECO:0000313|EMBL:ABU95432.1};
DE   Flags: Fragment;
OS   Sawyeria marylandensis.
OC   Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC   Psalteriomonadidae; Sawyeria.
OX   NCBI_TaxID=194530 {ECO:0000313|EMBL:ABU95432.1};
RN   [1] {ECO:0000313|EMBL:ABU95432.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=21037180; DOI=10.1128/EC.00122-10;
RA   Barbera M.J., Ruiz-Trillo I., Tufts J.Y., Bery A., Silberman J.D.,
RA   Roger A.J.;
RT   "Sawyeria marylandensis (Heterolobosea) has a hydrogenosome with novel
RT   metabolic properties.";
RL   Eukaryot. Cell 9:1913-1924(2010).
CC   -!- SIMILARITY: Belongs to the succinate/malate CoA ligase alpha subunit
CC       family. {ECO:0000256|RuleBase:RU000677}.
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DR   EMBL; EF612760; ABU95432.1; -; mRNA.
DR   AlphaFoldDB; D7EYH9; -.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 1.
DR   HAMAP; MF_01988; Succ_CoA_alpha; 1.
DR   InterPro; IPR017440; Cit_synth/succinyl-CoA_lig_AS.
DR   InterPro; IPR033847; Citrt_syn/SCS-alpha_CS.
DR   InterPro; IPR003781; CoA-bd.
DR   InterPro; IPR005810; CoA_lig_alpha.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR005811; SUCC_ACL_C.
DR   InterPro; IPR016102; Succinyl-CoA_synth-like.
DR   NCBIfam; TIGR01019; sucCoAalpha; 1.
DR   PANTHER; PTHR11117:SF2; SUCCINATE--COA LIGASE [ADP_GDP-FORMING] SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11117; SUCCINYL-COA LIGASE SUBUNIT ALPHA; 1.
DR   Pfam; PF02629; CoA_binding; 1.
DR   Pfam; PF00549; Ligase_CoA; 1.
DR   PIRSF; PIRSF001553; SucCS_alpha; 1.
DR   PRINTS; PR01798; SCOASYNTHASE.
DR   SMART; SM00881; CoA_binding; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 1.
DR   PROSITE; PS01216; SUCCINYL_COA_LIG_1; 1.
DR   PROSITE; PS00399; SUCCINYL_COA_LIG_2; 1.
PE   2: Evidence at transcript level;
KW   Ligase {ECO:0000256|RuleBase:RU000677};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          22..118
FT                   /note="CoA-binding"
FT                   /evidence="ECO:0000259|SMART:SM00881"
FT   ACT_SITE        267
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001553-1"
FT   NON_TER         307
FT                   /evidence="ECO:0000313|EMBL:ABU95432.1"
SQ   SEQUENCE   307 AA;  32285 MW;  99B0BF5B88DA9636 CRC64;
     MLKNLTKFFS ATSVALTKPY VLINKDTKVI CQGITGNQGS FHSQQMINYG TKMVGGVNPK
     KVGEKHLGLP IFKDVRQAVK ETGCHASMVF VPPPAGAAAI MEGIEAEIPL IVCITEGIPQ
     HDMVKVVSAL KTQKKTRLVG PNCPGVIKPN ECKIGIMPGY IHKKGKIGIV SRSGTLTYEA
     VSQTTAAGLG QSTVVGIGGD PFNGTNFIDV LDMFLHDPET EGIIMIGEIG GQAEEMAAHF
     LDISPIKKPV VGFIAGVTAP PGRRMGHAGA VISGGNGDAK SIMAAMEKVG IRMSATPAKM
     GTTMVQY
//
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