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Database: UniProt
Entry: V5G520_ANOGL
LinkDB: V5G520_ANOGL
Original site: V5G520_ANOGL 
ID   V5G520_ANOGL            Unreviewed;       310 AA.
AC   V5G520;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Succinate-CoA ligase subunit beta {ECO:0000256|RuleBase:RU361258};
DE            EC=6.2.1.- {ECO:0000256|RuleBase:RU361258};
GN   Name=SUCB2 {ECO:0000313|EMBL:JAB65155.1};
OS   Anoplophora glabripennis (Asian longhorn beetle) (Anoplophora nobilis).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Chrysomeloidea; Cerambycidae; Lamiinae; Lamiini; Anoplophora.
OX   NCBI_TaxID=217634 {ECO:0000313|EMBL:JAB65155.1};
RN   [1] {ECO:0000313|EMBL:JAB65155.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Scully E.D., Hoover K., Carlson J.E., Tien M., Geib S.M.;
RT   "Midgut Transcriptome Profiling of Anoplphora glabripennis, a
RT   Lignocellulose Degrading, Wood-Boring Cerambycid.";
RL   Submitted (JUL-2013) 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; GALX01003311; JAB65155.1; -; Transcribed_RNA.
DR   AlphaFoldDB; V5G520; -.
DR   EnsemblMetazoa; XM_018720542.1; XP_018576058.1; LOC108914690.
DR   UniPathway; UPA00223; UER00999.
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}.
FT   DOMAIN          1..128
FT                   /note="ATP-grasp fold succinyl-CoA synthetase-type"
FT                   /evidence="ECO:0000259|Pfam:PF08442"
FT   DOMAIN          187..307
FT                   /note="ATP-citrate synthase/succinyl-CoA ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00549"
SQ   SEQUENCE   310 AA;  33763 MW;  4AFDE0BACBD2F0D6 CRC64;
     MLGHKLITKQ TPRDGILVNK IMIAQSVNIK RETYFCILMD RQRNGPVIIA SPSGGVDIEA
     VAEKTPHLIK NVPVDIFKGV TDQMADELAE FLEFKGLLKQ KASNEIKKLW KLFLSVDATQ
     LEINPLVETD DNQVISVDAK LNFDDNAQFR QKEIFSAEDT SENDPREVEA SKYNLNYIGM
     TGNIGCLVNG AGLAMATMDI IKLHGGDPAN FLDVGGGVKE DQVRAAFRII TSDEKVKAIL
     VNVFGGIVNC VTIANGIVGA LKTMSLKVPL VVRLEGTNAD EARRIIKESG LNIRTAVDLE
     DAAKKAVASV
//
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