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Database: UniProt
Entry: A0A077DFS7_9BURK
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ID   A0A077DFS7_9BURK        Unreviewed;       866 AA.
AC   A0A077DFS7;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=aconitate hydratase {ECO:0000256|ARBA:ARBA00012926};
DE            EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
GN   ORFNames=IX83_00605 {ECO:0000313|EMBL:AIL32023.1};
OS   Basilea psittacipulmonis DSM 24701.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Basilea.
OX   NCBI_TaxID=1072685 {ECO:0000313|EMBL:AIL32023.1, ECO:0000313|Proteomes:UP000028945};
RN   [1] {ECO:0000313|EMBL:AIL32023.1, ECO:0000313|Proteomes:UP000028945}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 24701 {ECO:0000313|EMBL:AIL32023.1,
RC   ECO:0000313|Proteomes:UP000028945};
RX   PubMed=24581117; DOI=10.1186/1471-2164-15-169;
RA   Whiteson K.L., Hernandez D., Lazarevic V., Gaia N., Farinelli L.,
RA   Francois P., Pilo P., Frey J., Schrenzel J.;
RT   "A genomic perspective on a new bacterial genus and species from the
RT   Alcaligenaceae family, Basilea psittacipulmonis.";
RL   BMC Genomics 15:169-169(2014).
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   -!- 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}.
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DR   EMBL; CP009238; AIL32023.1; -; Genomic_DNA.
DR   RefSeq; WP_038497958.1; NZ_CP009238.1.
DR   AlphaFoldDB; A0A077DFS7; -.
DR   STRING; 1072685.IX83_00605; -.
DR   KEGG; bpsi:IX83_00605; -.
DR   eggNOG; COG1048; Bacteria.
DR   HOGENOM; CLU_013476_2_1_4; -.
DR   OrthoDB; 9764318at2; -.
DR   Proteomes; UP000028945; Chromosome.
DR   GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019679; P:propionate metabolic process, methylcitrate cycle; IEA:InterPro.
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; IPR012708; 2Me_IsoCit_deHydtase_FeS-dep.
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; TIGR02333; 2met_isocit_dHY; 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   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028945}.
FT   DOMAIN          60..536
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          659..791
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   866 AA;  95768 MW;  C3F9304D8EB33EB5 CRC64;
     MMSNRQLLPQ SHRYYYDAKK LCDEIKPNAY EQLPYTCKIL AENIVRKAEG RYEEDQINTW
     LNELIEHKKE IDFPWYPARV VCHDILGQTA LVDLAGLRDA IAEKGGDPSK VNPVVQTQLI
     VDHSLAVEYG GDDPDAFEKN RSIEDRRNED RFHFINWTKT AFENVDVIPA GNGIMHQINL
     EKMSPVIQVN GDTAFPDSCV GTDSHTPHTD ALGVISIGVG GLEAETVMLG RACMMRVPDI
     IGIHLTGKRQ PGITATDIVL ALTEFLRKEK VVGAFLEFFG EGADSLTIGD RATISNMTPE
     YGATAALFYI DQQTLDYLTL TGRDPQQVAL VKEYAQATGL WSEMMKTAVY PRTLSFDLSK
     VERNIAGPSH PHARLSTRDL KTKGIAKPHT QINNEIPDGA VIIAAITSCT NTSNPRNVIA
     AGLLARNANR RGLTRKPWVK SSFAPGSKVA EMYLNEAGLL KEMETLGFGV VAFACTTCNG
     MSGALDPAIQ KEIIERDVYT TAVLSGNRNF DGRIHPYAKQ AFLASPPLVI AYAIAGNIHV
     DIEQDSLGQD KNGSDVYLKD IWPDDHEIDE IVKTFVKPQQ FNAVYTPMFA SKTINKTTHP
     LYDWKKDSTY ISRPPYWNSE LSQPRSLKGM RPLAILPDNI TTDHLSPSNA ILPNSAAGEY
     LSKMGLAEED FNSYATHRGD HHTAQRATLA NPKLFNEMVK DEHGQTIQGS LTRIEPEGKI
     SRIWEAIETY QSRQQPLIII AGADYGQGSS RDWAAKGVRL AGVQAIVAEG FERIHRSNLV
     GMGILPLQFE AGTNRHTLKL DGTELYDVIG TPQAKGSLTL KITRQNGQID LIPVHCCLNT
     DEETLVYEAG GVLPRFAQDF LATHSK
//
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