SUCD_METJA
ID SUCD_METJA Reviewed; 294 AA.
AC Q58643;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Succinate--CoA ligase [ADP-forming] subunit alpha {ECO:0000255|HAMAP-Rule:MF_01988};
DE EC=6.2.1.5 {ECO:0000255|HAMAP-Rule:MF_01988};
DE AltName: Full=Succinyl-CoA synthetase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01988};
DE Short=SCS-alpha {ECO:0000255|HAMAP-Rule:MF_01988};
GN Name=sucD {ECO:0000255|HAMAP-Rule:MF_01988}; OrderedLocusNames=MJ1246;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS).
RA Niwa H., Kuramitsu S., Yokoyama S.;
RT "Crystal structure of succinyl-CoA synthetase alpha chain from
RT Methanocaldococcus jannaschii DSM 2661.";
RL Submitted (APR-2007) to the PDB data bank.
CC -!- FUNCTION: Succinyl-CoA synthetase functions in the citric acid cycle
CC (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of
CC either ATP or GTP and thus represents the only step of substrate-level
CC phosphorylation in the TCA. The alpha subunit of the enzyme binds the
CC substrates coenzyme A and phosphate, while succinate binding and
CC nucleotide specificity is provided by the beta subunit.
CC {ECO:0000255|HAMAP-Rule:MF_01988}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01988};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
CC from succinyl-CoA (ligase route): step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_01988}.
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits.
CC {ECO:0000255|HAMAP-Rule:MF_01988}.
CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase alpha subunit
CC family. {ECO:0000255|HAMAP-Rule:MF_01988}.
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DR EMBL; L77117; AAB99250.1; -; Genomic_DNA.
DR PIR; E64455; E64455.
DR PDB; 2YV1; X-ray; 1.70 A; A=1-294.
DR PDBsum; 2YV1; -.
DR AlphaFoldDB; Q58643; -.
DR SMR; Q58643; -.
DR STRING; 243232.MJ_1246; -.
DR EnsemblBacteria; AAB99250; AAB99250; MJ_1246.
DR KEGG; mja:MJ_1246; -.
DR eggNOG; arCOG01339; Archaea.
DR HOGENOM; CLU_052104_0_0_2; -.
DR InParanoid; Q58643; -.
DR OMA; VIICITE; -.
DR PhylomeDB; Q58643; -.
DR UniPathway; UPA00223; UER00999.
DR EvolutionaryTrace; Q58643; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0009361; C:succinate-CoA ligase complex (ADP-forming); IBA:GO_Central.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IBA:GO_Central.
DR GO; GO:0004776; F:succinate-CoA ligase (GDP-forming) activity; IBA:GO_Central.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR Gene3D; 3.40.50.261; -; 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; IPR005811; CoA_ligase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR Pfam; PF02629; CoA_binding; 1.
DR Pfam; PF00549; Ligase_CoA; 1.
DR PIRSF; PIRSF001553; SucCS_alpha; 1.
DR SMART; SM00881; CoA_binding; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF52210; SSF52210; 1.
DR TIGRFAMs; TIGR01019; sucCoAalpha; 1.
DR PROSITE; PS01216; SUCCINYL_COA_LIG_1; 1.
DR PROSITE; PS00399; SUCCINYL_COA_LIG_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Ligase; Nucleotide-binding; Reference proteome;
KW Tricarboxylic acid cycle.
FT CHAIN 1..294
FT /note="Succinate--CoA ligase [ADP-forming] subunit alpha"
FT /id="PRO_0000102810"
FT ACT_SITE 251
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01988"
FT BINDING 22..25
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01988"
FT BINDING 48
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01988"
FT BINDING 101..103
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01988"
FT BINDING 164
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit beta"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01988"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:2YV1"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:2YV1"
FT HELIX 24..35
FT /evidence="ECO:0007829|PDB:2YV1"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:2YV1"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:2YV1"
FT HELIX 62..69
FT /evidence="ECO:0007829|PDB:2YV1"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:2YV1"
FT HELIX 80..92
FT /evidence="ECO:0007829|PDB:2YV1"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:2YV1"
FT HELIX 107..120
FT /evidence="ECO:0007829|PDB:2YV1"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:2YV1"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:2YV1"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:2YV1"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:2YV1"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:2YV1"
FT STRAND 150..158
FT /evidence="ECO:0007829|PDB:2YV1"
FT HELIX 161..172
FT /evidence="ECO:0007829|PDB:2YV1"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:2YV1"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:2YV1"
FT HELIX 193..201
FT /evidence="ECO:0007829|PDB:2YV1"
FT STRAND 207..218
FT /evidence="ECO:0007829|PDB:2YV1"
FT HELIX 219..227
FT /evidence="ECO:0007829|PDB:2YV1"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:2YV1"
FT HELIX 263..273
FT /evidence="ECO:0007829|PDB:2YV1"
FT HELIX 283..292
FT /evidence="ECO:0007829|PDB:2YV1"
SQ SEQUENCE 294 AA; 30923 MW; 97BAAE1C0D311E6D CRC64;
MVLRDKMILL DENTKAIVQG ITGRQGSFHT KKMLECGTKI VGGVTPGKGG QNVHGVPVFD
TVKEAVKETD ANASVIFVPA PFAKDAVFEA IDAGIELIVV ITEHIPVHDT MEFVNYAEDV
GVKIIGPNTP GIASPKVGKL GIIPMEVLKE GSVGMVSRSG TLTYEIAHQI KKAGFGVSTC
VGIGGDPIVG LRYKEVLDLF EKDDETEAIV MIGEIGGGAE EEAAKFIEKM KKPVIGYIAG
QSAPEGKRMG HAGAIVEKGK GTAESKMKAL EEAGAYVAKN ISDIPKLLAG ILGK
