ID A0A1J8Q8A4_9GAMM Unreviewed; 910 AA.
AC A0A1J8Q8A4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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 ORFNames=QHL1GM_09530 {ECO:0000313|EMBL:OJA05610.1};
OS Halomonas sp. QHL1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1123773 {ECO:0000313|EMBL:OJA05610.1, ECO:0000313|Proteomes:UP000183854};
RN [1] {ECO:0000313|EMBL:OJA05610.1, ECO:0000313|Proteomes:UP000183854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QHL1 {ECO:0000313|EMBL:OJA05610.1,
RC ECO:0000313|Proteomes:UP000183854};
RA Seilhamer J.J.;
RL Submitted (AUG-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 -!- 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OJA05610.1}.
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DR EMBL; MINL01000001; OJA05610.1; -; Genomic_DNA.
DR RefSeq; WP_071694277.1; NZ_MINL01000001.1.
DR AlphaFoldDB; A0A1J8Q8A4; -.
DR STRING; 1123773.QHL1GM_09530; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000183854; 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 GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR CDD; cd01586; AcnA_IRP; 1.
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; 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}.
FT DOMAIN 73..581
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 709..836
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 910 AA; 99009 MW; 30011F7C557A732A CRC64;
MSKIPDTLST LEVGSKTYHY YSLPQAAETL GSIDRLPKTL KILLENQLRF ADDESVDQED
MQALVDWQTE GKSSREIGYR PARVLMQDFT GVPGVVDLAS MRAAVESLGE DPAKINPLSP
VDLVIDHSVM VDKFGNPAAF QENVDIEMQR NRERYEFLRW GQQAFDNFSV VPPGTGICHQ
VNLEYLGRTV WIKDEDGKTF AYPDTLVGTD SHTTMINGLG VLGWGVGGIE AEAAMLGQPV
SMLIPEVIGF KLTGKLREGI TATDLVLTVT EMLRKKGVVG KFVEFYGDGL KDLPLADRAT
IANMAPEYGA TCGFFPVDDE TLNYMRLTGR EDEQVALVEA YSKAQGLWRE PNDEPIFTDA
LELDMTEVEA SLAGPKRPQD RVALQDMAAA FDKFMQEDVK ADSTAKGKFS SEGGQTAVGV
ERSFEHDTSQ AVKLDDHDFS LDPGAVVIAA ITSCTNTSNP SVMMAAGLLA RKAREKGLTT
KPWVKTSLAP GSKVVTDYLE AAELNDDLDA LGFNLVGYGC TTCIGNSGPL PDEIEKAINS
GDLAVASVLS GNRNFEGRVH PLVKTNWLAS PPLVVAYALA GNVQLDLTQE PLGNDSNGDP
VYLKDIWPSQ AEIASAVEQV NTAMFRKEYG AVFEGDDVWK AIDVSESKVY QWPESTYIQH
PPFFEGMGRE PDAIEDVHSA RVLAMLGDSV TTDHISPAGA IKPDSPAGRY LQEHGVKPVD
FNSYGSRRGN HEVMMRGTFA NVRIKNEMLD GVVGGETRHV PSGEQMAIYD AAMKYKEEGK
PLVVIAGKEY GTGSSRDWAA KGTRLLGVRA VIAESFERIH RSNLIGMGVV PLQFAEGESR
QTLGLTGDEE ISIAGLSDLT PGGTVKIVIK NADGERSVDA KCRIDTVNEL AYYRHGGILH
YVLRKMIGAA
//
