GenomeNet

Database: UniProt
Entry: A0A0Q8R7D3_9SPHN
LinkDB: A0A0Q8R7D3_9SPHN
Original site: A0A0Q8R7D3_9SPHN 
ID   A0A0Q8R7D3_9SPHN        Unreviewed;       427 AA.
AC   A0A0Q8R7D3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Citrate synthase {ECO:0000256|PIRNR:PIRNR001369, ECO:0000256|RuleBase:RU003370};
GN   Name=gltA {ECO:0000313|EMBL:KRB90119.1};
GN   ORFNames=ASE22_14510 {ECO:0000313|EMBL:KRB90119.1};
OS   Sphingomonas sp. Root720.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1736595 {ECO:0000313|EMBL:KRB90119.1, ECO:0000313|Proteomes:UP000051570};
RN   [1] {ECO:0000313|Proteomes:UP000051570}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root720 {ECO:0000313|Proteomes:UP000051570};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRB90119.1, ECO:0000313|Proteomes:UP000051570}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root720 {ECO:0000313|EMBL:KRB90119.1,
RC   ECO:0000313|Proteomes:UP000051570};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + H2O + oxaloacetate = citrate + CoA + H(+);
CC         Xref=Rhea:RHEA:16845, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16452, ChEBI:CHEBI:16947, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288; EC=2.3.3.16;
CC         Evidence={ECO:0000256|ARBA:ARBA00000308,
CC         ECO:0000256|RuleBase:RU003370};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC       from oxaloacetate: step 1/2. {ECO:0000256|ARBA:ARBA00004751,
CC       ECO:0000256|RuleBase:RU003370}.
CC   -!- SIMILARITY: Belongs to the citrate synthase family.
CC       {ECO:0000256|ARBA:ARBA00010566, ECO:0000256|PIRNR:PIRNR001369,
CC       ECO:0000256|RuleBase:RU003406}.
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:KRB90119.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LMID01000012; KRB90119.1; -; Genomic_DNA.
DR   RefSeq; WP_056361672.1; NZ_LMID01000012.1.
DR   AlphaFoldDB; A0A0Q8R7D3; -.
DR   STRING; 1736595.ASE22_14510; -.
DR   UniPathway; UPA00223; UER00717.
DR   Proteomes; UP000051570; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004108; F:citrate (Si)-synthase activity; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR   CDD; cd06114; EcCS_like; 1.
DR   Gene3D; 2.20.28.60; -; 1.
DR   Gene3D; 1.10.580.10; Citrate Synthase, domain 1; 1.
DR   Gene3D; 1.10.230.10; Cytochrome P450-Terp, domain 2; 1.
DR   InterPro; IPR016142; Citrate_synth-like_lrg_a-sub.
DR   InterPro; IPR016143; Citrate_synth-like_sm_a-sub.
DR   InterPro; IPR002020; Citrate_synthase.
DR   InterPro; IPR019810; Citrate_synthase_AS.
DR   InterPro; IPR024176; Citrate_synthase_bac-typ.
DR   InterPro; IPR036969; Citrate_synthase_sf.
DR   InterPro; IPR010953; Citrate_synthase_typ-I.
DR   NCBIfam; TIGR01798; cit_synth_I; 1.
DR   PANTHER; PTHR42871; CITRATE SYNTHASE; 1.
DR   PANTHER; PTHR42871:SF1; CITRATE SYNTHASE; 1.
DR   Pfam; PF00285; Citrate_synt; 1.
DR   PIRSF; PIRSF001369; Citrate_synth; 1.
DR   PRINTS; PR00143; CITRTSNTHASE.
DR   SUPFAM; SSF48256; Citrate synthase; 1.
DR   PROSITE; PS00480; CITRATE_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000313|EMBL:KRB90119.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051570};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR001369};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW   ECO:0000256|RuleBase:RU003370}.
FT   TRANSMEM        363..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   ACT_SITE        305
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001369-1"
FT   ACT_SITE        362
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001369-1"
SQ   SEQUENCE   427 AA;  47246 MW;  69227D7FD76DDC24 CRC64;
     MADNVKLELG GKTSEYPVLS GTVGPDVVDI RKLYAATGAF TYDPGFTSTA SCQSAITYID
     GDEGVLLHRG YPIDQLAEQS SFMEVSYLLL NGQLPSAKEL EDFTYTISRH TMLHEQLATF
     YRGFRRDAHP MAIMCGVVGA LSAFYHDSTD INDPKQRMIA SHRLIAKMPT IAAMAYKYSV
     GQPFLYPKND LSYTGNFLRM TFGVPAEEYE IDPVIESAMD KIFILHADHE QNASTSTVRL
     AGSSGANPFA CIAAGIACLW GPAHGGANEA ALNMLREIGT PDRIPEYIAR AKNKDDPFRL
     MGFGHRVYKN FDPRAKVLGK AATEVLDKLG INDPVLDTAR ELEQIALKDQ YFIDKKLYPN
     VDFYSGVILS AIGFPTTMFT VLFALARTVG WVAQWNEMIS DPEQKIGRPR QLYTGAANRD
     YVPVSQR
//
DBGET integrated database retrieval system