ID U2J0Z6_9SPHI Unreviewed; 447 AA.
AC U2J0Z6;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Citrate synthase {ECO:0000256|PIRNR:PIRNR001369, ECO:0000256|RuleBase:RU003370};
GN Name=gltA {ECO:0000313|EMBL:ERJ58614.1};
GN ORFNames=M472_07530 {ECO:0000313|EMBL:ERJ58614.1};
OS Sphingobacterium paucimobilis HER1398.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=1346330 {ECO:0000313|EMBL:ERJ58614.1, ECO:0000313|Proteomes:UP000016584};
RN [1] {ECO:0000313|EMBL:ERJ58614.1, ECO:0000313|Proteomes:UP000016584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HER1398 {ECO:0000313|EMBL:ERJ58614.1,
RC ECO:0000313|Proteomes:UP000016584};
RX PubMed=23929486;
RA White R.A.III., Suttle C.A.;
RT "The Draft Genome Sequence of Sphingomonas paucimobilis Strain HER1398
RT (Proteobacteria), Host to the Giant PAU Phage, Indicates That It Is a
RT Member of the Genus Sphingobacterium (Bacteroidetes).";
RL Genome Announc. 1:e00598-13(2013).
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:ERJ58614.1}.
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DR EMBL; ATDL01000016; ERJ58614.1; -; Genomic_DNA.
DR AlphaFoldDB; U2J0Z6; -.
DR STRING; 1346330.M472_07530; -.
DR PATRIC; fig|1346330.5.peg.3169; -.
DR eggNOG; COG0372; Bacteria.
DR UniPathway; UPA00223; UER00717.
DR Proteomes; UP000016584; Unassembled WGS sequence.
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 Acyltransferase {ECO:0000313|EMBL:ERJ58614.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000016584};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR001369};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW ECO:0000256|RuleBase:RU003370}.
FT REGION 425..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 326
FT /evidence="ECO:0000256|PIRSR:PIRSR001369-1"
FT ACT_SITE 383
FT /evidence="ECO:0000256|PIRSR:PIRSR001369-1"
SQ SEQUENCE 447 AA; 50518 MW; 3BBBD7644CECE220 CRC64;
MGCFVIDFYI FVNTHRNLIM SETASFTLDG NTFEFPVITG TENEKAIDIS KLRDQSGYIT
LDPGFKNTGA TKSAITFLDG EKGILKYRGY KIEDLAEKST FLEVAYLLIF GNLPSKDILE
QFRTDIKRQM MVHEDMKMFF SGFPSKSHPM GQLSCLVGAL SAFYPESLNP NQSEEEEYKT
IINLLGKMPT IVSWIQKKSL GHPVVYPKKD LGYIDNFMNM IFGEVNCDKI FDEAVLDAMR
ILLILHADHE QNCSTSTVRI VGSSNANLYA SVSAGINALW GPLHGGANQA VIEMLEDIKN
DGGDVEKYLA KAKDKNDPFR LMGFGHRVYK NFDPRAKIIK KACDDVLEKL GVEDPVLDIA
KGLEKAALSD QYFIDRKLYP NVDFYSGIIY RALGFKSDMF TVLFALGRLP GWIAQWKEMR
DNKEPIGRPR QVYTGETSRQ YPDTDHR
//
