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Database: UniProt
Entry: G9MQE6_HYPVG
LinkDB: G9MQE6_HYPVG
Original site: G9MQE6_HYPVG 
ID   G9MQE6_HYPVG            Unreviewed;       394 AA.
AC   G9MQE6;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=ATP-grasp domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=TRIVIDRAFT_190926 {ECO:0000313|EMBL:EHK24067.1};
OS   Hypocrea virens (strain Gv29-8 / FGSC 10586) (Gliocladium virens)
OS   (Trichoderma virens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=413071 {ECO:0000313|EMBL:EHK24067.1, ECO:0000313|Proteomes:UP000007115};
RN   [1] {ECO:0000313|EMBL:EHK24067.1, ECO:0000313|Proteomes:UP000007115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Gv29-8 / FGSC 10586 {ECO:0000313|Proteomes:UP000007115};
RX   PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA   Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA   Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA   Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA   Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA   McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA   Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA   Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA   Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA   Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA   Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA   Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA   Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA   Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT   "Comparative genome sequence analysis underscores mycoparasitism as the
RT   ancestral life style of Trichoderma.";
RL   Genome Biol. 12:R40.1-R40.15(2011).
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
CC       from succinyl-CoA (ligase route): step 1/1.
CC       {ECO:0000256|ARBA:ARBA00005064}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHK24067.1}.
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DR   EMBL; ABDF02000005; EHK24067.1; -; Genomic_DNA.
DR   RefSeq; XP_013958266.1; XM_014102791.1.
DR   AlphaFoldDB; G9MQE6; -.
DR   STRING; 413071.G9MQE6; -.
DR   EnsemblFungi; EHK24067; EHK24067; TRIVIDRAFT_190926.
DR   GeneID; 25789493; -.
DR   VEuPathDB; FungiDB:TRIVIDRAFT_190926; -.
DR   eggNOG; KOG2799; Eukaryota.
DR   HOGENOM; CLU_037430_1_0_1; -.
DR   InParanoid; G9MQE6; -.
DR   OMA; RFWFNLS; -.
DR   OrthoDB; 1384037at2759; -.
DR   UniPathway; UPA00223; UER00999.
DR   Proteomes; UP000007115; 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   PANTHER; PTHR11815:SF19; SUCCINATE--COA LIGASE [ADP-FORMING] SUBUNIT BETA; 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   4: Predicted;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007115}.
FT   DOMAIN          17..209
FT                   /note="ATP-grasp fold succinyl-CoA synthetase-type"
FT                   /evidence="ECO:0000259|Pfam:PF08442"
FT   DOMAIN          269..373
FT                   /note="ATP-citrate synthase/succinyl-CoA ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00549"
SQ   SEQUENCE   394 AA;  43127 MW;  233026E59B0AE1C6 CRC64;
     MAIRRKTYSE LCVGYAQVPR GILVRTPLEA QDAVKSLGKN CIFRAQVLCG HSGKLLFEDG
     LRGGIQTVEN LEQGLDLATR MLNRQVTSEN IHHRSLTVNQ VLVSESLVHE DQWHLVMTID
     RENYCPVVII SKYNDSASQD EQMPQNVSEK EFSFTFSFSQ GITEDLVSRI STSLGVGREE
     MTNLADVLTN LYKIFREKDA TLLEISPLAR LSTGLFACLD ATLVVDDDAA KRQPDIFRLR
     DTTQEVHDEV RAEQHSLVYI KMDGNIGNIV NGAGLAMVTN DAIGLHGGAS ANFLDAGGQA
     TKETMIQALG IVMGDERVKA ILINIYGGIT RCDMIAESII GAAQEMTLAV PLVVRLQGTN
     STEGLKLLAD ARLGLHVESD FGRAAQRAVE LAQP
//
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