ID C5C5L0_BEUC1 Unreviewed; 914 AA.
AC C5C5L0;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 84.
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 OrderedLocusNames=Bcav_1946 {ECO:0000313|EMBL:ACQ80201.1};
OS Beutenbergia cavernae (strain ATCC BAA-8 / DSM 12333 / NBRC 16432).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Beutenbergiaceae;
OC Beutenbergia.
OX NCBI_TaxID=471853 {ECO:0000313|EMBL:ACQ80201.1, ECO:0000313|Proteomes:UP000007962};
RN [1] {ECO:0000313|EMBL:ACQ80201.1, ECO:0000313|Proteomes:UP000007962}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-8 / DSM 12333 / NBRC 16432
RC {ECO:0000313|Proteomes:UP000007962};
RX PubMed=21304633; DOI=10.4056/sigs.1162;
RA Land M., Pukall R., Abt B., Goker M., Rohde M., Glavina Del Rio T.,
RA Tice H., Copeland A., Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D.,
RA Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA Pati A., Chen A., Palaniappan K., Hauser L., Chang Y.J., Jefferies C.C.,
RA Saunders E., Brettin T., Detter J.C., Han C., Chain P., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Lapidus A.;
RT "Complete genome sequence of Beutenbergia cavernae type strain (HKI
RT 0122).";
RL Stand. Genomic Sci. 1:21-28(2009).
CC -!- FUNCTION: Catalyzes the isomerization of citrate to isocitrate via cis-
CC aconitate. {ECO:0000256|RuleBase:RU361275}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = 2-methyl-cis-
CC aconitate + H2O; Xref=Rhea:RHEA:17941, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57429, ChEBI:CHEBI:57872; EC=4.2.1.99;
CC Evidence={ECO:0000256|ARBA:ARBA00000118};
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 -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC {ECO:0000256|ARBA:ARBA00005026}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185, ECO:0000256|RuleBase:RU361275}.
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DR EMBL; CP001618; ACQ80201.1; -; Genomic_DNA.
DR RefSeq; WP_015882441.1; NC_012669.1.
DR AlphaFoldDB; C5C5L0; -.
DR STRING; 471853.Bcav_1946; -.
DR KEGG; bcv:Bcav_1946; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_013476_2_1_11; -.
DR OMA; NGGIMQY; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000007962; Chromosome.
DR GO; GO:0047456; F:2-methylisocitrate dehydratase activity; IEA:UniProtKB-EC.
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; 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; CITRATE HYDRO-LYASE; 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, ECO:0000313|EMBL:ACQ80201.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000007962}.
FT DOMAIN 71..580
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 710..837
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 914 AA; 98086 MW; FB63E87FB8128674 CRC64;
MSSVDTFGAK GTLAVGGRSY EIFRLSAVPG VERLPFSLKV LAENLLRTED GANITADHVR
ALAAWDPDAE PDTEIQFTPA RVVMQDFTGV PCVVDLATMR EAVTSLGGEA STINPLAPAE
LVIDHSVQID VFGTSDAFAR NVEYEYQRNG ERYQFLRWGQ TAFDDFKVVP PGTGIVHQVN
IEYLARVVMT REVDGVERAY PDTCVGTDSH TTMVNGLGVL GWGVGGIEAE AAMLGQPVSM
LIPRVVGFKL SGEIPAGVTA TDVVLTITQK LRQHGVVGKF VEFYGDGVAA VPLANRATIG
NMSPEFGSTA AIFPIDDVTL EYLRLTGRSG DQVALVEAYA KEQGLWHDPA SEPVFSEYLE
LDLSTVVPSI AGPKRPQDRI ELSRAKEQFA RDLPAYAPEA TNGVDEAEEE SFPASDSPAI
SSHVHRTVPV TTPDGVTYDL FHGAVVIASI TSCTNTSNPS VMLAAALLAK NAVEKGLTVK
PWVKTSMAPG SQVVTNYYEK AGLWPYLEKL GYHLVGYGCT TCIGNSGPLP DEVSEAVNTH
DLAVASVLSG NRNFEGRINP DVKMNYLASP PLVIAYALAG TMDFDFEADP LGRDADGHPI
FLRDLWPTPE EVQATIDSSI TREMFTADYA DVFAGDDLWR ALDTPEGDTF AWDPESTYVR
KPPYFEGMGA EPEPVTDIAG ARVLAKLGDS VTTDHISPAG SIKADSPAGR YLAEHGVERR
DFNSYGSRRG NHEVMIRGTF ANIRLKNQLL DGVEGGFTRN LLSGEQTSIY DAAQAYAEAG
VPLVVLGGKE YGSGSSRDWA AKGTSLLGVR AVITESFERI HRSNLIGMGV LPLQFPDGET
ADSLGLDGTE TFDVAGITEL NSGTTPSTVR VTATKADGTA VEFDAVVRID TPGEADYYRN
GGILQYVLRS LVAA
//