SUCB1_MESAU
ID SUCB1_MESAU Reviewed; 221 AA.
AC P86226;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial {ECO:0000250|UniProtKB:Q9YI37};
DE EC=6.2.1.5 {ECO:0000250|UniProtKB:Q9YI37};
DE AltName: Full=ATP-specific succinyl-CoA synthetase subunit beta {ECO:0000250|UniProtKB:Q9YI37};
DE Short=A-SCS {ECO:0000250|UniProtKB:Q9YI37};
DE AltName: Full=Succinyl-CoA synthetase beta-A chain {ECO:0000250|UniProtKB:Q9YI37};
DE Short=SCS-betaA {ECO:0000250|UniProtKB:Q9YI37};
DE Flags: Fragments;
GN Name=Sucla2 {ECO:0000250|UniProtKB:Q9YI37};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20400973; DOI=10.1038/aja.2010.19;
RA Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.;
RT "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen
RT (GP96) are unique to hamster caput epididymal spermatozoa.";
RL Asian J. Androl. 12:344-355(2010).
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:0000250|UniProtKB:Q9YI37}.
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:0000250|UniProtKB:Q9YI37};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
CC from succinyl-CoA (ligase route): step 1/1.
CC {ECO:0000250|UniProtKB:Q9YI37}.
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:Q9YI37}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9YI37}.
CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta subunit
CC family. ATP-specific subunit beta subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; P86226; -.
DR SMR; P86226; -.
DR UniPathway; UPA00223; UER00999.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.261; -; 1.
DR InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type.
DR InterPro; IPR005809; Succ_CoA_synthase_bsu.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR PANTHER; PTHR11815; PTHR11815; 4.
DR Pfam; PF08442; ATP-grasp_2; 1.
DR SUPFAM; SSF52210; SSF52210; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Ligase; Mitochondrion; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Tricarboxylic acid cycle.
FT CHAIN <1..221
FT /note="Succinate--CoA ligase [ADP-forming] subunit beta,
FT mitochondrial"
FT /id="PRO_0000394309"
FT DOMAIN <1..122
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 5
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0A836"
FT BINDING 171..173
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000250|UniProtKB:P0A836"
FT SITE 1
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000250|UniProtKB:P53590"
FT MOD_RES 22
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2I9"
FT MOD_RES 26
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2R7"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2I9"
FT MOD_RES 139
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2I9"
FT MOD_RES 196
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2I9"
FT NON_CONS 13..14
FT /evidence="ECO:0000305"
FT NON_CONS 22..23
FT /evidence="ECO:0000305"
FT NON_CONS 43..44
FT /evidence="ECO:0000305"
FT NON_CONS 84..85
FT /evidence="ECO:0000305"
FT NON_CONS 109..110
FT /evidence="ECO:0000305"
FT NON_CONS 121..122
FT /evidence="ECO:0000305"
FT NON_CONS 134..135
FT /evidence="ECO:0000305"
FT NON_CONS 160..161
FT /evidence="ECO:0000305"
FT NON_CONS 174..175
FT /evidence="ECO:0000305"
FT NON_CONS 184..185
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 221 AA; 24249 MW; 22894FDA430F8A83 CRC64;
DVVIKAQVLA GGRIVFSPEE AKLITKQTGA KGRICNQVLV CERREYYFAI TMERSFQGPV
LIGSAQGGVN IEDVAAENPE AIVKKMGFPS NIVDSAAENM IKLYNLFLKI NFDSNSAYRQ
KIFDLQDWSQ EDERLHGGTP ANFLDVGGGA TVQQVTEAFK VQAILVNIFG GIMRLQGTRV
DDAKILACDD LDEAAKMVVK LSEIVTLAKE AHVDVKFQLP I
