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Database: UniProt
Entry: A0A093ETL5_TYTAL
LinkDB: A0A093ETL5_TYTAL
Original site: A0A093ETL5_TYTAL 
ID   A0A093ETL5_TYTAL        Unreviewed;       366 AA.
AC   A0A093ETL5;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 24.
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=N341_05015 {ECO:0000313|EMBL:KFV48637.1};
OS   Tyto alba (Barn owl).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Strigiformes; Tytonidae; Tyto.
OX   NCBI_TaxID=56313 {ECO:0000313|EMBL:KFV48637.1, ECO:0000313|Proteomes:UP000054190};
RN   [1] {ECO:0000313|EMBL:KFV48637.1, ECO:0000313|Proteomes:UP000054190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N341 {ECO:0000313|EMBL:KFV48637.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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; KK381525; KFV48637.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093ETL5; -.
DR   UniPathway; UPA00223; UER00999.
DR   Proteomes; UP000054190; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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   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; IPR005809; Succ_CoA_ligase-like_bsu.
DR   InterPro; IPR016102; Succinyl-CoA_synth-like.
DR   NCBIfam; TIGR01016; sucCoAbeta; 1.
DR   PANTHER; PTHR11815:SF21; SUCCINATE--COA LIGASE [GDP-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:UP000054190}.
FT   DOMAIN          10..216
FT                   /note="ATP-grasp fold succinyl-CoA synthetase-type"
FT                   /evidence="ECO:0000259|Pfam:PF08442"
FT   DOMAIN          278..366
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:KFV48637.1"
FT   NON_TER         366
FT                   /evidence="ECO:0000313|EMBL:KFV48637.1"
SQ   SEQUENCE   366 AA;  39983 MW;  08DCB3F48C7EBD0E CRC64;
     VQLTPRRWLN LQEYQSKKIM ADHGVTVQRF FVADSANDAL EAAQRLKAKE IVLKAQILAG
     GRGKGIFNSG LKGGVHLTKD PKIVEQLAKQ MIGYNLSTKQ TSKDGVTVKK VMVAEALNIS
     RETYFAILMD RACNGPVMVG SPQGGVDIEE VAVTSPELIF KEEIDIFEGI KDHQALQMAK
     NLGFKVPLQE QAADQIKKLY NLFLKIDATQ VEVNPFGETP EGQVVCFDAK INFDDNAEFR
     QKEIFAMDDK SENEPMENEA AKYDLKYIGL DGNIACFVNG AGLAMATCDI ISLNGGKPAN
     FLDLGGGVKE AQVYQAFKLL TADPKVEAIL VNIFGGIVNC AIIANGITKA CRELELKVPL
     VVRLEG
//
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