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Database: UniProt
Entry: A0A093J1J9_FULGA
LinkDB: A0A093J1J9_FULGA
Original site: A0A093J1J9_FULGA 
ID   A0A093J1J9_FULGA        Unreviewed;       374 AA.
AC   A0A093J1J9;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 25.
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=N327_00868 {ECO:0000313|EMBL:KFW07788.1};
OS   Fulmarus glacialis (Northern fulmar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Procellariiformes; Procellariidae;
OC   Fulmarus.
OX   NCBI_TaxID=30455 {ECO:0000313|EMBL:KFW07788.1, ECO:0000313|Proteomes:UP000053806};
RN   [1] {ECO:0000313|EMBL:KFW07788.1, ECO:0000313|Proteomes:UP000053806}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N327 {ECO:0000313|EMBL:KFW07788.1};
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; KK603710; KFW07788.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093J1J9; -.
DR   UniPathway; UPA00223; UER00999.
DR   Proteomes; UP000053806; 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_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:UP000053806};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          1..173
FT                   /note="ATP-grasp fold succinyl-CoA synthetase-type"
FT                   /evidence="ECO:0000259|Pfam:PF08442"
FT   DOMAIN          232..352
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:KFW07788.1"
FT   NON_TER         374
FT                   /evidence="ECO:0000313|EMBL:KFW07788.1"
SQ   SEQUENCE   374 AA;  40697 MW;  EBC21A2C5C1EE1DD CRC64;
     LGSKDLVVKA QVLAGGRGKG TFEGGLKGGV KIVFSPEEAK DISSKMIGKK LFTKQTGEKG
     RICNQVFICE RRYPRREYYF AITMERSFQG PVLIGSSQGG VNIEDVAAEN PDAIIKEPID
     IVEGIKKEQA VRLAQKMGFP PNLVDEAAEN MIKLYNLFLK YDATMIEINP MVEDASGIVM
     CMDAKINFDS NSAYRQKKIF DMQDWTQEDQ RDRDAAKADL NYIGLDGNIG CLVNGAGLAM
     ATMDIIKLHG GTPANFLDVG GGATVQQVTE AFKLITSDKK VLAILVNIFG GIMRCDVIAQ
     GIVMAVKDLD LKIPIVVRLQ GTRVDDAKAL ITASGLKILA CDDLDEAAKM VVKLSEIVSL
     AKQAQVDVKF QLPI
//
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