ID A0A1G8N1Q0_9RHOO Unreviewed; 872 AA.
AC A0A1G8N1Q0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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 ORFNames=SAMN05660652_03961 {ECO:0000313|EMBL:SDI73530.1};
OS Propionivibrio dicarboxylicus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Propionivibrio.
OX NCBI_TaxID=83767 {ECO:0000313|EMBL:SDI73530.1, ECO:0000313|Proteomes:UP000198607};
RN [1] {ECO:0000313|EMBL:SDI73530.1, ECO:0000313|Proteomes:UP000198607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5885 {ECO:0000313|EMBL:SDI73530.1,
RC ECO:0000313|Proteomes:UP000198607};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FNCY01000027; SDI73530.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8N1Q0; -.
DR STRING; 83767.SAMN05660652_03961; -.
DR OrthoDB; 9764318at2; -.
DR Proteomes; UP000198607; Unassembled WGS sequence.
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 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; 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:SF43; 2-METHYLCITRATE DEHYDRATASE (2-METHYL-TRANS-ACONITATE FORMING); 1.
DR PANTHER; PTHR11670; ACONITASE/IRON-RESPONSIVE ELEMENT FAMILY MEMBER; 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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000198607}.
FT DOMAIN 73..545
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 669..796
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 872 AA; 93005 MW; ED0F2CC9930813EF CRC64;
METQWCEGPV SRSGELSQNG VRSVALRAQI ESLYPGAFAR LPLTCRIFAE NVLRRCAPEA
RAAALAQIVG QRDDADFPFY PARVVLQDIL GGTALVDMAG LRDAVAEAGG DPRRVNPVVP
AQLVIDHSLN VEFSGAEPDA LEKNMAVEAR RNAERFEFMA WAQKAFDNVN VVMQGNGILH
QINLEYFSPV VQCEDGVLFP DTLVGTDSHT PMVNALGVLG WGVGGIEAES VMLGRPIWMR
VPAIVGVELS GQRQPGIQAT DLVLALTEFL RAQGVVGAIL EFYGPGVASL SVPDRATIAN
MSPEFGATAS LFAIDAQTID YLRLTGRSDE VIERTEAYAR AQGLWADALT QAEYKRTLRF
DLATVGRAIA GPANPHQRIP LASLASAGIA RPAAERDAIA DGGPLPEGAV VIAAITSCTN
TSNPRNLVTA ALLARNAAAR GLSPKSWVKT SFAPGSRAVA GYLGAAGLLE PLRQLGFGIV
GFACTSCNGM SGPLAPAIEA EILKRALPTA AVLSGNRNFN GRIHPRVSEA FIASPALVVA
YALAGSIRVD VEHEALGVDA KGLPVLLSEL WPEDAEVEAI MAAHVSGEHF RSAYAAVCGA
DTSADAPVSP QFAWREESTY IRRPPYWKTV LTQLPRATSM RPIVILGDNV TTDDLSPSGT
ILPESAAGQY LLAQGTTKEE FNTYTTRRGD HIVAVRATFA NNRLRNEMCP GIEGPVTRVE
PEGTIMPIFD AAQQYIEREQ ELIVIAGRNY GCGSSRDWAA KGVRLIGVRA VVAESFERIH
RTNLVGMGVL PLEFTDGATR KTLALDGSET YALRGFDGAP APGALLTLAI TRRDGSVIEM
TVRSRIDTDD ECRLFAAGGL LPCIANELLG RS
//
