ID B2JTI6_PARP8 Unreviewed; 874 AA.
AC B2JTI6;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 82.
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=Bphy_6878 {ECO:0000313|EMBL:ACC75889.1};
OS Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS STM815) (Burkholderia phymatum).
OG Plasmid pBPHY01 {ECO:0000313|EMBL:ACC75889.1,
OG ECO:0000313|Proteomes:UP000001192}.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=391038 {ECO:0000313|EMBL:ACC75889.1, ECO:0000313|Proteomes:UP000001192};
RN [1] {ECO:0000313|Proteomes:UP000001192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815
RC {ECO:0000313|Proteomes:UP000001192};
RC PLASMID=Plasmid pBPHY01 {ECO:0000313|Proteomes:UP000001192};
RX PubMed=25197461; DOI=10.4056/sigs.4861021;
RA Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A., Melkonian R.,
RA James E.K., Young J.P., Bena G., Hauser L., Land M., Kyrpides N., Bruce D.,
RA Chain P., Copeland A., Pitluck S., Woyke T., Lizotte-Waniewski M.,
RA Bristow J., Riley M.;
RT "Complete genome sequence of Burkholderia phymatum STM815(T), a broad host
RT range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL Stand. Genomic Sci. 9:763-774(2014).
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 -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185, ECO:0000256|RuleBase:RU361275}.
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DR EMBL; CP001045; ACC75889.1; -; Genomic_DNA.
DR RefSeq; WP_012406048.1; NZ_CADFGH010000012.1.
DR AlphaFoldDB; B2JTI6; -.
DR KEGG; bph:Bphy_6878; -.
DR HOGENOM; CLU_013476_2_1_4; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000001192; Plasmid pBPHY01.
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 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; 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|ARBA:ARBA00022485, 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|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU361275};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Plasmid {ECO:0000313|EMBL:ACC75889.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001192}.
FT DOMAIN 65..542
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 670..795
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 874 AA; 94328 MW; 27BBE1D749F3CEDA CRC64;
MENTYSPTEA RLSVDGVSHR YVDLPGLFGD KLRELPVVLR LLLENVIRNT QGEERRQAVE
GILAWTARAT SEAEIAFQPN RVLMHDTTST PALVDIAGMR DALAEAGADP ATLNPVLPVD
SSVDHSLAVE YFAQRDAAPL NLKLELRRNA ERYRFLRWAS KALKGVRIHP PGTGIMHTIN
LEQLATVVTS VERDGEKWAV PDTLIGTDSH TPMINGIGVL GWGVGGLEAQ TVMFGMPVMQ
RIPDVIGVRL TGAMQPGVLA TDLALTVTQR LRAIGVSGEF VEFFGPGVTT LSAGDRAVVA
NMAPEYGAST GFFPIDQHTL DYLRSTNRAE TSIKLVEAFA RRTGTWFEPQ AEPRYTRTID
IDLASIGMHI AGPRRPQDLI DYSQTATTLA KLDFQSAQPH RSMPKHPVAI AAITSCTNTS
DPALLIAAGL LARKARALGL SVPSWVKTSL GPGSPAAAAY LERAGLIDDL SAVGFDIVGY
GCTTCIGNSG PLTEPIRAAL AQKSIYPVAM LSGNRNFPGR IHPDLDLGFI MSPPLVIAFA
LAADAEKDLS VDPIQQTSDG KPVYLRDLWP TRDEVDALVR AAADPQDYPR AFALASQNPA
WHDLDAPDNA RFPWNPASTA LRRPPFASAT QGSQLGRYSA YPLLVLGDDV TTDHISPASA
IPKDSFVADF LVSRGDDRDD LNVFASRRGN WEVMMRAAFY NRTLVNSLRA GMPVAHTLHV
PSGDVMPIFE AAQRYRDDGD SVVLVAGERY GTGSSRDWAA KGQRLLGIRA VLAVSFERIH
RSNLIGMGIL PLRFAGGANP NTLELQPGDK LEVDAVSDTL SPRCRVAVRV VRANGSVQPI
EATAAVETQL ECTLLRSGGV IPLILQKSLQ AQEA
//
