ID Q5M3U3_STRT2 Unreviewed; 887 AA.
AC Q5M3U3;
DT 01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 01-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 119.
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 Name=citB {ECO:0000313|EMBL:AAV60900.1};
GN OrderedLocusNames=stu1268 {ECO:0000313|EMBL:AAV60900.1};
OS Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=264199 {ECO:0000313|EMBL:AAV60900.1, ECO:0000313|Proteomes:UP000001170};
RN [1] {ECO:0000313|EMBL:AAV60900.1, ECO:0000313|Proteomes:UP000001170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-250 / LMG 18311 {ECO:0000313|Proteomes:UP000001170};
RX PubMed=15543133; DOI=10.1038/nbt1034;
RA Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D.,
RA Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M.,
RA Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D.,
RA Hancy F., Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.;
RT "Complete sequence and comparative genome analysis of the dairy bacterium
RT Streptococcus thermophilus.";
RL Nat. Biotechnol. 22:1554-1558(2004).
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; CP000023; AAV60900.1; -; Genomic_DNA.
DR RefSeq; WP_011226167.1; NC_006448.1.
DR AlphaFoldDB; Q5M3U3; -.
DR STRING; 264199.stu1268; -.
DR GeneID; 66899057; -.
DR KEGG; stl:stu1268; -.
DR PATRIC; fig|264199.4.peg.1250; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_013476_2_1_9; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000001170; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001170}.
FT DOMAIN 73..559
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 687..813
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 887 AA; 97831 MW; D9220E4D53D1E7DB CRC64;
MQEYCSNLTV NGKIFSFYDL EKAAKSYDVK VEELPYSIRI LLESLLRKKD GIDVKESHIS
DLIKFPNFPT ISEIPFKPSR VILQDFTGVP VVVDLASMRD AIVANGGKAE LINPEIPVDL
VIDHSVQVDS YGCDTALEDN INLEFKRNNE RYEFLKWAEQ SFENYRAVPP ATGIIHQVNI
EFLSDVIIEK DGLLYPDSMF GTDSHTTMIN GIGVLGWGVG GIEAEAAMLG EASYFPIPEV
IGVHLTGELP KIATATDLAL KITQVLRSEN VVGKFVEYFG SGLKSLSLAD RATIANMAPE
YGATCGYFPI DDETLNYMRL TNRDEEHIQV TEAYTKANHL FYDPSKEAKY TKVVEIDLST
IKPSISGPKR PQDLILLSDA KQEFQDAVVR EAGVRGFGLD KKELEKTAKV DFEDHSETIQ
TGHVAIAAIT SCTNTSNPYV LMAAGLLAKK AVEKGLKVSP TVKTSLAPGS KVVTGYLKAS
GLQSYLDKLG FNLVGYGCTT CIGNSGDLRS EVAKAIVDTD LLASAVLSGN RNFEGRINPL
VKANFLASPP LVVAYALAGN TNIDLTREPL GFDDNGRAVY LEDIMPSRDE IEAYVDKYVT
RQLFRDEYAS VFSDSEKWNA ITTEQSQNYK WNEKSTYIQN PPYFDALGDD LTIKPLNNLK
VLAKFGDTVT TDHISPAGNI ARNSPASRYL SENGVDYQEF NSYGSRRGNH EVMMRGTFAN
IRIKNELAEG KIGGYTKYEG DILPIYDAAM KYKEANRDTL VIAGKDYGMG SSRDWAAKGA
NLLGVKVVLA ESFERIHRSN LVMMGILPVQ FMEGENAETL GLTGHEIFSF DLSENPGVHD
VITVTASTPE QTKTFKVLVR FDADADIRYY KNGGILPMVV RKKLKGA
//
