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Database: UniProt
Entry: F4G9S8_ALIDK
LinkDB: F4G9S8_ALIDK
Original site: F4G9S8_ALIDK 
ID   F4G9S8_ALIDK            Unreviewed;       431 AA.
AC   F4G9S8;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=Citrate synthase {ECO:0000256|PIRNR:PIRNR001369, ECO:0000256|RuleBase:RU003370};
GN   OrderedLocusNames=Alide2_2209 {ECO:0000313|EMBL:AEB84578.1};
OS   Alicycliphilus denitrificans (strain DSM 14773 / CIP 107495 / K601).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Alicycliphilus.
OX   NCBI_TaxID=596154 {ECO:0000313|EMBL:AEB84578.1, ECO:0000313|Proteomes:UP000007938};
RN   [1] {ECO:0000313|EMBL:AEB84578.1, ECO:0000313|Proteomes:UP000007938}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14773 / CIP 107495 / K601
RC   {ECO:0000313|Proteomes:UP000007938};
RX   PubMed=21742888; DOI=10.1128/JB.00365-11;
RA   Oosterkamp M.J., Veuskens T., Plugge C.M., Langenhoff A.A., Gerritse J.,
RA   van Berkel W.J., Pieper D.H., Junca H., Goodwin L.A., Daligault H.E.,
RA   Bruce D.C., Detter J.C., Tapia R., Han C.S., Land M.L., Hauser L.J.,
RA   Smidt H., Stams A.J.;
RT   "Genome Sequences of Alicycliphilus denitrificans Strains BC and K601T.";
RL   J. Bacteriol. 193:5028-5029(2011).
RN   [2] {ECO:0000313|EMBL:AEB84578.1, ECO:0000313|Proteomes:UP000007938}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14773 / CIP 107495 / K601
RC   {ECO:0000313|Proteomes:UP000007938};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Zeytun A., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Oosterkamp M.,
RA   Pieper D., van Berkel W., Langenhoff A., Smidt H., Stams A., Woyke T.;
RT   "Complete sequence of chromosome of Alicycliphilus denitrificans K601.";
RL   Submitted (APR-2011) 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}.
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DR   EMBL; CP002657; AEB84578.1; -; Genomic_DNA.
DR   RefSeq; WP_013518795.1; NC_015422.1.
DR   AlphaFoldDB; F4G9S8; -.
DR   STRING; 596154.Alide2_2209; -.
DR   KEGG; adk:Alide2_2209; -.
DR   eggNOG; COG0372; Bacteria.
DR   HOGENOM; CLU_025068_0_0_4; -.
DR   OrthoDB; 9800864at2; -.
DR   UniPathway; UPA00223; UER00717.
DR   Proteomes; UP000007938; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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   Reference proteome {ECO:0000313|Proteomes:UP000007938};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR001369};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW   ECO:0000256|RuleBase:RU003370}.
FT   ACT_SITE        313
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001369-1"
FT   ACT_SITE        371
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001369-1"
SQ   SEQUENCE   431 AA;  47958 MW;  4828995EF46062B7 CRC64;
     MKLADNKATL SFSNGSPSVE LPVYQGSIGP DVIDIRKLYG QTGMFTYDPG FLSTASCQSA
     ITYIDGDKGE LLYRGYPIEQ LATKCDYLDT CYLLLNGELP NAGQRDDFHK LVLKHTMVHE
     QMQFFLRGFR RDAHPMAVLT GLIGALSAFY HDSTDINNPE HRHISAIRLI SKLPTLVAMA
     YKYGVGQPFM YPRNELSYAG NFLRMMFGTP CEDYKVNPVI ERAMDRIFIL HADHEQNAST
     STVRLCGSSG TNPFAAIAAG VACLWGPAHG GANEACLNML EHLQANGGVA KVGEFMEQVK
     DKNSGVKLMG FGHRVYKNYD PRAKLMQETC NEVLAELGLE KDPLFALAKQ LEKIALEDDY
     FVQRKLYPNV DFYSGIVQRA IGIPVNLFTG IFALARTVGW IAQLNEMIGD PEYKIGRPRQ
     LFTGSPRRDV P
//
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