ID A0A0D5M505_9GAMM Unreviewed; 869 AA.
AC A0A0D5M505;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=KO116_02847 {ECO:0000313|EMBL:AJY51320.1};
OS Halomonas sp. KO116.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1504981 {ECO:0000313|EMBL:AJY51320.1, ECO:0000313|Proteomes:UP000028645};
RN [1] {ECO:0000313|EMBL:AJY51320.1, ECO:0000313|Proteomes:UP000028645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KO116 {ECO:0000313|EMBL:AJY51320.1,
RC ECO:0000313|Proteomes:UP000028645};
RX PubMed=25953187;
RA O'Dell K.B., Woo H.L., Utturkar S., Klingeman D., Brown S.D., Hazen T.C.;
RT "Genome Sequence of Halomonas sp. Strain KO116, an Ionic Liquid-Tolerant
RT Marine Bacterium Isolated from a Lignin-Enriched Seawater Microcosm.";
RL Genome Announc. 3:0-0(2015).
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; CP011052; AJY51320.1; -; Genomic_DNA.
DR RefSeq; WP_035566641.1; NZ_CP011052.1.
DR AlphaFoldDB; A0A0D5M505; -.
DR STRING; 1504981.KO116_02847; -.
DR KEGG; hak:KO116_02847; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_013476_2_1_6; -.
DR OrthoDB; 9764318at2; -.
DR Proteomes; UP000028645; 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 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 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, ECO:0000313|EMBL:AJY51320.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 66..538
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 662..793
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 869 AA; 94766 MW; 9D4EB2618CA4554F CRC64;
MNTQYRKPLP GTALEFFDAR EAVEDIQPGA YAKLPYTSRV LAEQLVRRCD PDLLTDALKQ
LIERRSDLDF PWYPARVVCH DILGQTALVD LAGLRDAIAE KGGDPAKVNP VVPTQLIVDH
SLAVEHAGSE EGAFEKNRAI EDRRNDDRFH FINWTKTAFE NVDVIPPGNG IMHQINLEKM
SPVVQNRDGI AYPDTCVGTD SHTPMVDALG VISVGVGGLE AESVMLGRAS MMRLPDIVGV
ELTGKLQPGI TGTDMVLAIT EFLRKERVVG AYLEFYGEGA DALTVGDRAT ISNMTPEYGA
TAAMFYIDGQ TIDYLKITGR EDEQVALVET YAKHTGLWAD SLTEVEYERV LTFDLSSVTR
TLAGPSNPHA HLPTSELAQR GIAVGLEAAQ AEEKAGKMPD GAVIIAAITS CTNTSNPRNM
VAAGLIARNA NRLGLLRKPW VKSSLAPGSK TVKMYLEEAG LMSELENLGF GVVAYACTTC
NGMSGALDPK IQQEIIERDL YATAVLSGNR NFDGRIHPHA QQAFLASPPL VVAYAIAGTI
RFDIEKDVLG VDQAGNPVTL KDIWPADEEI DAIVKSSVKP EQFRQTYIPM FDLDKSARAQ
VSPLYDWRPQ STYIRRPPYW EGNMAKVRTL KGMRPLAILP DNITTDHLSP SNAIQLNSAA
GEYLAKMGLP EEDFNSYATH RGDHLTAQRA TFANPKLFNE MVRDADGNVK QGSLARVEPE
GQVTRMWEAI ETYMARKQPL IIIAGADYGQ GSSRDWAAKG VALAGVEAIA AEGFERIHRT
NLIGMGVMPL EFEPGTTRMT LGLDGTETFD VEGAVSPGAM LTLVIHRQNG ESERVAVKCR
LDTAEEVSIY TAGGVLQRFA QDFLESTAA
//
