ID A0A091G1I7_9AVES Unreviewed; 435 AA.
AC A0A091G1I7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Succinate-CoA ligase subunit beta {ECO:0000256|RuleBase:RU361258};
DE EC=6.2.1.- {ECO:0000256|RuleBase:RU361258};
DE Flags: Fragment;
GN ORFNames=N303_09086 {ECO:0000313|EMBL:KFO75261.1};
OS Cuculus canorus (common cuckoo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO75261.1, ECO:0000313|Proteomes:UP000053760};
RN [1] {ECO:0000313|EMBL:KFO75261.1, ECO:0000313|Proteomes:UP000053760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO75261.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00043683};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
CC from succinyl-CoA (ligase route): step 1/1.
CC {ECO:0000256|ARBA:ARBA00005064}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC {ECO:0000256|RuleBase:RU361258}.
CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta subunit
CC family. {ECO:0000256|RuleBase:RU361258}.
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DR EMBL; KL447613; KFO75261.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091G1I7; -.
DR STRING; 55661.A0A091G1I7; -.
DR UniPathway; UPA00223; UER00999.
DR Proteomes; UP000053760; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 1.
DR HAMAP; MF_00558; Succ_CoA_beta; 1.
DR HAMAP; MF_03220; Succ_CoA_betaA_euk; 1.
DR InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR017866; Succ-CoA_synthase_bsu_CS.
DR InterPro; IPR005811; SUCC_ACL_C.
DR InterPro; IPR034723; Succ_CoA_betaA_euk.
DR InterPro; IPR005809; Succ_CoA_ligase-like_bsu.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR NCBIfam; TIGR01016; sucCoAbeta; 1.
DR PANTHER; PTHR11815:SF10; SUCCINATE--COA LIGASE [ADP-FORMING] SUBUNIT BETA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11815; SUCCINYL-COA SYNTHETASE BETA CHAIN; 1.
DR Pfam; PF08442; ATP-grasp_2; 1.
DR Pfam; PF00549; Ligase_CoA; 1.
DR PIRSF; PIRSF001554; SucCS_beta; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 1.
DR PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU361258};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU361258};
KW Reference proteome {ECO:0000313|Proteomes:UP000053760};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 27..234
FT /note="ATP-grasp fold succinyl-CoA synthetase-type"
FT /evidence="ECO:0000259|Pfam:PF08442"
FT DOMAIN 293..413
FT /note="ATP-citrate synthase/succinyl-CoA ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00549"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO75261.1"
FT NON_TER 435
FT /evidence="ECO:0000313|EMBL:KFO75261.1"
SQ SEQUENCE 435 AA; 47387 MW; 0EBF9861DEA96B22 CRC64;
QVLGGSPGIL NNHGFQVQQQ QQRRLSLHEY LSMGLLQEAG IAVPHGLVAR TPDEAYKIAK
EIGSKDLVVK AQVLAGGRGK GTFEGGLKGG VKIVFSPEEA KDISSKMIGK KLFTKQTGEK
GRICNQVFIC ERRYPRREYY FAITMERSFQ GPVLIGSSQG GVNIEDVAAE NPDAIIKEPI
DIVEGIKKEQ AVRLAQKMGF PPNLVDEAAE NMIKLYNLFL KYDATMIEIN PMVEDASGVV
MCMDAKINFD SNSAYRQKKI FDMQDWTQED ERDRDAAKAD LNYIGLDGNI GCLVNGAGLA
MATMDIIKLH GGTPANFLDV GGGATVQQVT EAFKLITSDK KVLAILVNIF GGIMRCDVIA
QGIVMAVKDL DLKIPIVVRL QGTRVDDAKA LITASGLKIL ACDDLDEAAK MVVKLSEIVN
LAKQAQVDVK FQLPI
//
