ID E1R002_OLSUV Unreviewed; 892 AA.
AC E1R002;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Aconitate hydratase {ECO:0000256|ARBA:ARBA00012926, ECO:0000256|RuleBase:RU361275};
DE Short=Aconitase {ECO:0000256|RuleBase:RU361275};
DE EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926, ECO:0000256|RuleBase:RU361275};
GN OrderedLocusNames=Olsu_0853 {ECO:0000313|EMBL:ADK67966.1};
OS Olsenella uli (strain ATCC 49627 / DSM 7084 / CIP 109912 / JCM 12494 /
OS NCIMB 702895 / VPI D76D-27C) (Lactobacillus uli).
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC Olsenella.
OX NCBI_TaxID=633147 {ECO:0000313|EMBL:ADK67966.1, ECO:0000313|Proteomes:UP000000333};
RN [1] {ECO:0000313|EMBL:ADK67966.1, ECO:0000313|Proteomes:UP000000333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49627 / DSM 7084 / CIP 109912 / JCM 12494 / NCIMB 702895 /
RC VPI D76D-27C {ECO:0000313|Proteomes:UP000000333};
RX PubMed=21304694; DOI=10.4056/sigs.1082860;
RA Goker M., Held B., Lucas S., Nolan M., Yasawong M., Glavina Del Rio T.,
RA Tice H., Cheng J.F., Bruce D., Detter J.C., Tapia R., Han C., Goodwin L.,
RA Pitluck S., Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A.,
RA Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Rohde M., Sikorski J., Pukall R., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Complete genome sequence of Olsenella uli type strain (VPI D76D-27C).";
RL Stand. Genomic Sci. 3:76-84(2010).
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 -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185, ECO:0000256|RuleBase:RU361275}.
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DR EMBL; CP002106; ADK67966.1; -; Genomic_DNA.
DR RefSeq; WP_013251718.1; NZ_JQCO01000001.1.
DR AlphaFoldDB; E1R002; -.
DR STRING; 633147.Olsu_0853; -.
DR GeneID; 78512271; -.
DR KEGG; ols:Olsu_0853; -.
DR PATRIC; fig|633147.7.peg.695; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_013476_2_1_11; -.
DR OrthoDB; 9764318at2; -.
DR Proteomes; UP000000333; 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 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; 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.
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:ADK67966.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000000333}.
FT DOMAIN 78..562
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 690..816
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 892 AA; 93865 MW; 1AC0E64575860CCE CRC64;
MTATTDFERA VASARIPRPL CAGSLRRLVY DVSKIPGAAH LPRALVVLLE NCVRRATSDE
QATELARRVI EAGLAGAQGS EIEFMPARAL FQDFTGVPVF VDFAAMRDAV VERGGDPSRV
SPHIPCTLVV DHSVIADFTG SDDAAERNQR MEAERNHERF AFLKWAAHSF DNVRIVPPGS
GICHQLNMEH FCEVVCDDAL AGGDVPVACF DTLVGTDSHT TTANGLGVLG WGVGGIEAEA
AALGQPITML VPPVVELNLT GALNDGVSGM DLALTVAQVL RSEGVVGTLV EVGGPGVRTL
SATQRACVAN MTPEYGATTT LFPVDDRSIE YLALTGRDPE RIELARAYLE VQGVFGASEG
RRYARRISLD LSTVALSLAG PSRPHDRVSP AGLRERFRDA LASHGRAVGD LSFGYDTPEG
SVTLTHGTIA IAAITSCTTA TDPAMMVAAG LLARNAAGRG LAPKPWVKKV LAPGSHSTAL
LLSRAGLADA LSQLGFHTCG FGCMSCIGNS GDILPQLKGV AAKAELASVL SGNRNFEGRI
SPDVSQNYLC QPALVVAYSL VGTVDVDLSS DPVGIGTDGV PVMLSDILPT DEEITATLGS
FLDEGLFAQG GEGLFEGSAE WRRIDAGTSD VFSWDPDSTY VRRPPYFDLA THRDVVGISR
ARVLALLGDF VTTDHISPAG SIAADSPAGR YLVERGVSPA EFNTYGSRRG NHEVMARGTF
ANVKLSNALA QGRSGGLTTD LLDGEVKSIF DASVHYAEAG APLVIVAGKL YGSGSSRDWA
GKGPTLLGVR AVIAESFERI HRSNLVQMGV LPLQFVEGQS ASSLGLDGTE VFDVEAVDLS
AGMPTKREAV VTARRADGSG LRFECVVRVD TPMEGAFLAA GGILPYVLDQ LL
//
