SUCB1_PIG
ID SUCB1_PIG Reviewed; 425 AA.
AC O97580;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03220};
DE EC=6.2.1.5 {ECO:0000255|HAMAP-Rule:MF_03220};
DE AltName: Full=ATP-specific succinyl-CoA synthetase subunit beta {ECO:0000255|HAMAP-Rule:MF_03220};
DE Short=A-SCS {ECO:0000255|HAMAP-Rule:MF_03220};
DE AltName: Full=Succinyl-CoA synthetase beta-A chain {ECO:0000255|HAMAP-Rule:MF_03220};
DE Short=SCS-betaA {ECO:0000255|HAMAP-Rule:MF_03220};
DE Flags: Precursor; Fragment;
GN Name=SUCLA2 {ECO:0000255|HAMAP-Rule:MF_03220};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=9765291; DOI=10.1074/jbc.273.42.27580;
RA Johnson J.D., Mehus J.G., Tews K., Milavetz B.I., Lambeth D.O.;
RT "Genetic evidence for the expression of ATP- and GTP-specific succinyl-CoA
RT synthetases in multicellular eucaryotes.";
RL J. Biol. Chem. 273:27580-27586(1998).
CC -!- FUNCTION: ATP-specific succinyl-CoA synthetase functions in the citric
CC acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the
CC synthesis of ATP and thus represents the only step of substrate-level
CC phosphorylation in the TCA. The beta subunit provides nucleotide
CC specificity of the enzyme and binds the substrate succinate, while the
CC binding sites for coenzyme A and phosphate are found in the alpha
CC subunit. {ECO:0000255|HAMAP-Rule:MF_03220}.
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_03220};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03220};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03220};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
CC from succinyl-CoA (ligase route): step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_03220}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The beta subunit
CC determines specificity for ATP. Interacts with ALAS2 (By similarity).
CC {ECO:0000250|UniProtKB:Q9P2R7, ECO:0000255|HAMAP-Rule:MF_03220}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03220}.
CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta subunit
CC family. ATP-specific subunit beta subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_03220}.
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DR EMBL; AF061966; AAC69751.1; -; mRNA.
DR AlphaFoldDB; O97580; -.
DR SMR; O97580; -.
DR STRING; 9823.ENSSSCP00000010036; -.
DR iPTMnet; O97580; -.
DR PaxDb; O97580; -.
DR PeptideAtlas; O97580; -.
DR PRIDE; O97580; -.
DR eggNOG; KOG2799; Eukaryota.
DR InParanoid; O97580; -.
DR UniPathway; UPA00223; UER00999.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0042709; C:succinate-CoA ligase complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IBA:GO_Central.
DR GO; GO:0006104; P:succinyl-CoA metabolic process; IBA:GO_Central.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.40.50.261; -; 1.
DR HAMAP; MF_00558; Succ_CoA_beta; 1.
DR HAMAP; MF_03220; Succ_CoA_betaA_euk; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR005811; CoA_ligase.
DR InterPro; IPR017866; Succ-CoA_synthase_bsu_CS.
DR InterPro; IPR034723; Succ_CoA_betaA_euk.
DR InterPro; IPR005809; Succ_CoA_synthase_bsu.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR PANTHER; PTHR11815; PTHR11815; 1.
DR Pfam; PF08442; ATP-grasp_2; 1.
DR Pfam; PF00549; Ligase_CoA; 1.
DR PIRSF; PIRSF001554; SucCS_beta; 1.
DR SUPFAM; SSF52210; SSF52210; 1.
DR TIGRFAMs; TIGR01016; sucCoAbeta; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Ligase; Magnesium; Metal-binding; Mitochondrion;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transit peptide;
KW Tricarboxylic acid cycle.
FT TRANSIT <1..14
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 15..425
FT /note="Succinate--CoA ligase [ADP-forming] subunit beta,
FT mitochondrial"
FT /id="PRO_0000033354"
FT DOMAIN 23..250
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT BINDING 60
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT BINDING 67..69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT BINDING 220
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT BINDING 234
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT BINDING 285
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT BINDING 342..344
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT SITE 56
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT SITE 124
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT MOD_RES 40
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2R7"
FT MOD_RES 46
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2R7"
FT MOD_RES 50
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2I9"
FT MOD_RES 50
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2I9"
FT MOD_RES 91
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2I9"
FT MOD_RES 101
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2I9"
FT MOD_RES 105
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2R7"
FT MOD_RES 178
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2I9"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2I9"
FT MOD_RES 303
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2I9"
FT MOD_RES 330
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2I9"
FT MOD_RES 400
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2I9"
FT NON_TER 1
SQ SEQUENCE 425 AA; 46259 MW; 4FDD4F521BB68836 CRC64;
NNHGLQIQQQ QQRNLSLHEY MSMELLQEAG VSIPKGHVAK SPDEAYAIAK KLGSKDVVIK
AQVLAGGRGK GTFESGLKGG VKIVFSPEEA KAVSSQMIGK KLFTKQTGEK GRICNQVLVC
ERRYPRREYY FAITMERSFQ GPVLIGSSQG GVNIEDVAAE TPEAIVKEPI DIVEGIKKEQ
AVRLAQKMGF PPSIVDSAAE NMIKLYNLFL KYDATMVEIN PMVEDSDGAV LCMDAKINFD
SNSAYRQKKI FDLQDWTQED ERDKDAAKAN LNYIGLDGNI GCLVNGAGLA MATMDIIKLH
GGTPANFLDV GGGATVHQVT EAFKLITSDK KVLSILVNIF GGIMRCDVIA QGIVMAVKDL
EIKIPVVVRL QGTRVDDAKA LIADSGLKIL ACDDLDEAAK MVVKLSEIVT LTKQAQVDVK
FQLPI
