ID A0A160JIS2_9PROT Unreviewed; 443 AA.
AC A0A160JIS2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Citrate synthase {ECO:0000256|PIRNR:PIRNR001369, ECO:0000256|RuleBase:RU003370};
GN Name=gltA {ECO:0000313|EMBL:ANC92834.1};
GN ORFNames=A6A40_13645 {ECO:0000313|EMBL:ANC92834.1};
OS Azospirillum humicireducens.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=1226968 {ECO:0000313|EMBL:ANC92834.1, ECO:0000313|Proteomes:UP000077405};
RN [1] {ECO:0000313|EMBL:ANC92834.1, ECO:0000313|Proteomes:UP000077405}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SgZ-5 {ECO:0000313|EMBL:ANC92834.1,
RC ECO:0000313|Proteomes:UP000077405};
RX PubMed=23264502; DOI=10.1099/ijs.0.046813-0;
RA Zhou S., Han L., Wang Y., Yang G., Zhuang L., Hu P.;
RT "Azospirillum humicireducens sp. nov., a nitrogen-fixing bacterium isolated
RT from a microbial fuel cell.";
RL Int. J. Syst. Evol. Microbiol. 63:2618-2624(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}.
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DR EMBL; CP015285; ANC92834.1; -; Genomic_DNA.
DR RefSeq; WP_063635872.1; NZ_CP015285.1.
DR AlphaFoldDB; A0A160JIS2; -.
DR STRING; 1226968.A6A40_13645; -.
DR KEGG; ahu:A6A40_13645; -.
DR OrthoDB; 9800864at2; -.
DR UniPathway; UPA00223; UER00717.
DR Proteomes; UP000077405; 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 Acyltransferase {ECO:0000313|EMBL:ANC92834.1};
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 320
FT /evidence="ECO:0000256|PIRSR:PIRSR001369-1"
FT ACT_SITE 378
FT /evidence="ECO:0000256|PIRSR:PIRSR001369-1"
SQ SEQUENCE 443 AA; 49598 MW; AF3ACF7519FB60CE CRC64;
MESSKHTPHG DVIQVGTVTL TDDATGKTLK LPLLGGSTGP NVIDIRKLYA ETGYFTYDPG
FTSTAACDSA ITYIDGDEGV LLHRGYAIAD LAENCDFLEV CHLLLNGELP NPQQKSDFER
TITYHTMVHE QLAKFYSGFR RDAHPMAIMC GVVGALSAFY HDSTDIFDPV QRKIAAHRLI
AKMPTMAAMA HKYTVGEPFM YPRNDLTYAE NFLYMTFGTP CEEWTVDPVL SEAMDKIFIL
HADHEQNAST STVRLAGSSH ANPFACIASG IAALWGPAHG GANEAVLKML EEISSVDRIP
EFVRRAKDKN DSFRLMGFGH RVYKNYDPRA KIMRETCYQV LDRLGIQDEP HLAIAMELER
IALSDEYFIE KKLYPNVDFY SGIILKAMGF PTSMFTVLFA LARTVGWISQ WKEMIEDPAQ
KIGRPRQLFT GNPARPFVPL DKR
//
