probable citrate synthase, mitochondrial isoform X2 [Drosophila
LOCUS XP_022226639 464 aa linear INV 14-MAY-2021
obscura].
ACCESSION XP_022226639
VERSION XP_022226639.1
DBLINK BioProject: PRJNA728747
DBSOURCE REFSEQ: accession XM_022370947.2
KEYWORDS RefSeq.
SOURCE Drosophila obscura
ORGANISM Drosophila obscura
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Endopterygota; Diptera; Brachycera;
Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora.
COMMENT MODEL REFSEQ: This record is predicted by automated computational
analysis. This record is derived from a genomic sequence
(NW_024542752.1) annotated using gene prediction method: Gnomon.
Also see:
Documentation of NCBI's Annotation Process
##Genome-Annotation-Data-START##
Annotation Provider :: NCBI
Annotation Status :: Full annotation
Annotation Name :: Drosophila obscura Annotation
Release 101
Annotation Version :: 101
Annotation Pipeline :: NCBI eukaryotic genome annotation
pipeline
Annotation Software Version :: 8.6
Annotation Method :: Best-placed RefSeq; Gnomon
Features Annotated :: Gene; mRNA; CDS; ncRNA
##Genome-Annotation-Data-END##
COMPLETENESS: full length.
FEATURES Location/Qualifiers
source 1..464
/organism="Drosophila obscura"
/isolate="BZ-5 IFL"
/db_xref="taxon:7282"
/chromosome="Unknown"
/sex="male"
/tissue_type="whole fly"
/dev_stage="Adult fly"
/geo_loc_name="Serbia: Babin Zub"
/collection_date="2017"
Protein 1..464
/product="probable citrate synthase, mitochondrial isoform
X2"
/calculated_mol_wt=51502
Region 34..461
/region_name="ScCit1-2_like"
/note="Saccharomyces cerevisiae (Sc) citrate synthases
Cit1-2_like. Citrate synthases (CS) catalyzes the
condensation of acetyl coenzyme A (AcCoA) with
oxaloacetate (OAA) to form citrate and coenzyme A (CoA),
the first step in the citric acid cycle (TCA or...;
cd06105"
/db_xref="CDD:99858"
Site order(72..73,76..82,167,171,174,266,271,274..275,278..279,
282..284,288,295..296,299..301,349,446..454)
/site_type="other"
/note="dimer interface [polypeptide binding]"
/db_xref="CDD:99858"
Site order(74,266,270,300..303,305,308,342..349,352,357,398,
401,403,425,429,446,449)
/site_type="active"
/db_xref="CDD:99858"
Site order(74,300..302,305,308,342..349,352,398,401,403,446)
/site_type="other"
/note="coenzyme A binding site [chemical binding]"
/db_xref="CDD:99858"
Site order(74,266,270,301..302,342..343,345..349,357,401,429)
/site_type="other"
/note="citrylCoA binding site [chemical binding]"
/db_xref="CDD:99858"
Site order(266,270,302..303,348..349,357,403,425,429,449)
/site_type="other"
/note="oxalacetate/citrate binding site [chemical
binding]"
/db_xref="CDD:99858"
Site order(302,348,403)
/site_type="active"
/note="catalytic triad [active]"
/db_xref="CDD:99858"
CDS 1..464
/gene="LOC111076900"
/coded_by="XM_022370947.2:148..1542"
/db_xref="GeneID:111076900"
ORIGIN
1 mslyrisark lveaqklpnv gsyvrlisad grslrdvlna kvpeeqervk nfrkqhgatk
61 lgettidmmy ggmrgikalv tetsvldade girfrglsip ecqkvlpaap ggteplpegl
121 fwllltgevp sqaqvqqlsr ewaeraalpq hvvtmlnnmp tslhpmsqla aavtalnhds
181 kfakaysegv hkskyweyvy edsmdliakl pvvaatiycn tyrggkgsrs idssldwsan
241 fvkmlgydna qftelmrlyl tihsdheggn vsahtvhlvg salsdpylsf aagmnglagp
301 lhglanqevl vwlrklqkea gnnpseeqlk eyiwktlksg qvvpgyghav lrktdprytc
361 qrefalkhlp edelfqlvsk iykvvppilt etgkvknpwp nvdahsgvll qyfgmkemny
421 ytvlfgvsra lgvlaslvwd ralglpierp ksystdllvk mvqk