ID S5RH95_9STRE Unreviewed; 920 AA.
AC S5RH95;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Aconitate hydratase {ECO:0000256|RuleBase:RU361275};
DE Short=Aconitase {ECO:0000256|RuleBase:RU361275};
DE EC=4.2.1.3 {ECO:0000256|RuleBase:RU361275};
GN ORFNames=KE3_0653 {ECO:0000313|EMBL:AGS05161.1};
OS Streptococcus lutetiensis 033.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1076934 {ECO:0000313|EMBL:AGS05161.1, ECO:0000313|Proteomes:UP000015268};
RN [1] {ECO:0000313|EMBL:AGS05161.1, ECO:0000313|Proteomes:UP000015268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=033 {ECO:0000313|EMBL:AGS05161.1,
RC ECO:0000313|Proteomes:UP000015268};
RX PubMed=23782707; DOI=10.1186/1471-2180-13-141;
RA Jin D., Chen C., Li L., Lu S., Li Z., Zhou Z., Jing H., Xu Y., Du P.,
RA Wang H., Xiong Y., Zheng H., Bai X., Sun H., Wang L., Ye C., Gottschalk M.,
RA Xu J.;
RT "Dynamics of fecal microbial communities in children with diarrhea of
RT unknown etiology and genomic analysis of associated Streptococcus
RT lutetiensis.";
RL BMC Microbiol. 13:141-141(2013).
CC -!- FUNCTION: Catalyzes the isomerization of citrate to isocitrate via cis-
CC aconitate. {ECO:0000256|RuleBase:RU361275}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=citrate = D-threo-isocitrate; Xref=Rhea:RHEA:10336,
CC ChEBI:CHEBI:15562, ChEBI:CHEBI:16947; EC=4.2.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00023501,
CC ECO:0000256|RuleBase:RU361275};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 2/2. {ECO:0000256|ARBA:ARBA00004717}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185, ECO:0000256|RuleBase:RU361275}.
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DR EMBL; CP003025; AGS05161.1; -; Genomic_DNA.
DR AlphaFoldDB; S5RH95; -.
DR KEGG; slu:KE3_0653; -.
DR PATRIC; fig|1076934.5.peg.593; -.
DR HOGENOM; CLU_013476_2_1_9; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000015268; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR CDD; cd01586; AcnA_IRP; 1.
DR CDD; cd01580; AcnA_IRP_Swivel; 1.
DR Gene3D; 6.10.190.10; -; 1.
DR Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
DR InterPro; IPR044137; AcnA_IRP_Swivel.
DR InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR InterPro; IPR006249; Aconitase/IRP2.
DR InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR NCBIfam; TIGR01341; aconitase_1; 1.
DR PANTHER; PTHR11670; ACONITASE/IRON-RESPONSIVE ELEMENT FAMILY MEMBER; 1.
DR PANTHER; PTHR11670:SF54; CYTOPLASMIC ACONITATE HYDRATASE; 1.
DR Pfam; PF00330; Aconitase; 1.
DR Pfam; PF00694; Aconitase_C; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
DR SUPFAM; SSF52016; LeuD/IlvD-like; 1.
DR PROSITE; PS00450; ACONITASE_1; 1.
DR PROSITE; PS01244; ACONITASE_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|RuleBase:RU361275};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU361275};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU361275};
KW Lyase {ECO:0000256|RuleBase:RU361275};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 103..592
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 720..846
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 920 AA; 101663 MW; 70F6073209AFB2AB CRC64;
MSGNLTHVCK LMLAKFSEFC IIKNNIIIIG GPYMTEFLSN FSFKENDYSY LNLEEAVSHY
GGNIKRIPYT IRILLESLLR KYDGVDVTKS HIENLATYNP KNIQGEVPFK PSRVILQDFT
GVPVVVDLAS MRDAIVSNGG DADLINPEIP VDLVIDHSVQ VDFFGCDTAL EDNINMEFKR
NNERYEFLKW AEKSFDNYRA VPPATGIIHQ VNIEYLSDVI IEKDGMLYPD SMFGTDSHAT
MINGIGVLGW GVGGIEAEAA MLGEASFFPI PEVIGVRLTG KLPKIATATD LALKVTQVLR
QEKVVGKFVE YFGDGLSNLS LAERATIANM APEYGATCGY FPIDDETLNY MRLTNRDEDH
IALTKEYAKR NSLFYDPEHQ AEYTKVVEID LSSISPSISG PKRPQDLIDL TQAKQTFQES
LTREAGVQGF GLTADEINKT ATVHFEDQDV EIKTGHVAIA AITSCTNTSN PYVLMSAGLL
AKNAVERGLH VAPTVKTSLA PGSKVVTGYL RNSGLQTYLD TLGFNIVGYG CTTCIGNSGS
LRPEVAEAIT DTDLLASAVL SGNRNFEGRV NPLVKANFLA SPPLVVAYAL AGNTNIDLTT
EPLGFDQNNE PAYLKDIMPT NDEVAKYVDQ FVTRELFEHE YEHVFTDSEK WNQIPTEESK
IYHWNEASTY IQNPPYFDNL GDDLAIKPLK NLKPLVKFGD SVTTDHISPA GNIAKNSPAA
KYLTEHGVDY LDFNSYGSRR GNHEVMMRGT FANIRIQNQL ADGKIGGYTK YNGELMPIYD
AAMHYKEDKV DTLVIAGKDY GMGSSRDWAA KGSNLLGVKA VLAESFERIH RSNLVMMGVL
PLQFLEGDTA ENLGLTGYET YDINLSENPG IHDIVDVIVR DDSGEKHFKA MVRFDADADI
RYYKNGGILP MVVRKKLGGA
//
