SUCB1_BOVIN
ID SUCB1_BOVIN Reviewed; 463 AA.
AC Q148D5;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
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;
GN Name=SUCLA2 {ECO:0000255|HAMAP-Rule:MF_03220};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal pons;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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; BC118443; AAI18444.1; -; mRNA.
DR RefSeq; NP_001068961.1; NM_001075493.1.
DR AlphaFoldDB; Q148D5; -.
DR SMR; Q148D5; -.
DR STRING; 9913.ENSBTAP00000008894; -.
DR PaxDb; Q148D5; -.
DR PeptideAtlas; Q148D5; -.
DR PRIDE; Q148D5; -.
DR GeneID; 511090; -.
DR KEGG; bta:511090; -.
DR CTD; 8803; -.
DR eggNOG; KOG2799; Eukaryota.
DR InParanoid; Q148D5; -.
DR OrthoDB; 973871at2759; -.
DR UniPathway; UPA00223; UER00999.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
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..53
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT CHAIN 54..463
FT /note="Succinate--CoA ligase [ADP-forming] subunit beta,
FT mitochondrial"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT /id="PRO_0000383147"
FT DOMAIN 61..288
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT BINDING 98
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT BINDING 105..107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT BINDING 258
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT BINDING 272
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT BINDING 323
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT BINDING 380..382
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT SITE 94
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT SITE 162
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT MOD_RES 78
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2R7"
FT MOD_RES 84
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2R7"
FT MOD_RES 88
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2I9"
FT MOD_RES 88
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2I9"
FT MOD_RES 129
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2I9"
FT MOD_RES 139
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2I9"
FT MOD_RES 143
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2R7"
FT MOD_RES 216
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2I9"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2I9"
FT MOD_RES 341
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2I9"
FT MOD_RES 368
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2I9"
FT MOD_RES 438
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2I9"
SQ SEQUENCE 463 AA; 50130 MW; 770CE8CCE86AF001 CRC64;
MAASVFYSRL LAAATLRSHR PRTALPAAAQ VLGSSGLFNN HGVQIQHQQQ RNLSLHEYLS
MELLQEAGVS IPKGHVAKSP DEAYAIAKKL GSKDVVIKAQ VLAGGRGKGT FESGLKGGVK
IVFSPEEAKA VSSQMIGKKL FTKQTGEKGR ICNQVLVCER RYPRREYYFA ITMERSFQGP
VLIGSSHGGV NIEDVAAETP EAIVKEPIDI VEGIKKEQAV RLAQKMGFPA SIVDSAAENM
IKLYDPFLKY DATMVEINPM VEDSDGAVLC MDAKINFDSN SAYRQKKIFD LQDWTQEDER
DKDAAKADLN YIGLDGNIGC LVNGAGLAMA TMDIIKLHGG TPANFLDVGG GATVHQVTEA
FKLITSDKKV LSILVNIFGG IMRCDVIAQG IVMAVKDLEI KIPIVVRLQG TRVDDAKALI
ADSGLKILAC DDLDEAAKMV VKLSEIVTLA KQAQVDVKFQ LPI
