ID A0A109LWM9_9SPHN Unreviewed; 891 AA.
AC A0A109LWM9;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=ASS64_08095 {ECO:0000313|EMBL:KWV95130.1};
OS Erythrobacter sp. AP23.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=499656 {ECO:0000313|EMBL:KWV95130.1, ECO:0000313|Proteomes:UP000058666};
RN [1] {ECO:0000313|EMBL:KWV95130.1, ECO:0000313|Proteomes:UP000058666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP23 {ECO:0000313|EMBL:KWV95130.1,
RC ECO:0000313|Proteomes:UP000058666};
RA Lin W., Zheng Q.;
RT "Draft genome sequence of Erythrobacter sp. AP23.";
RL Submitted (NOV-2015) 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:KWV95130.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LNBY01000015; KWV95130.1; -; Genomic_DNA.
DR RefSeq; WP_067692962.1; NZ_LNBY01000015.1.
DR AlphaFoldDB; A0A109LWM9; -.
DR STRING; 499656.ASS64_08095; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000058666; 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..562
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 692..817
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 891 AA; 96391 MW; A7E1030FDBA69895 CRC64;
MTQVGKDTLG TRSTLTVNGK DYAYYSFAKA EEQIGDVSKL PFSLKVLLEN MLRFEDGGFT
VSTDDAQAIA DWQKNPATGK EIQYRPARVL LQDFTGVPCV VDLAAMRDAI SKLGGDTAKI
NPQVPVNLVI DHSVMVDEFG HPKAFEKNVE LEYARNAERY DFLKWGSKSF ENFSAVPPGT
GICHQVNLEY IGKGVWSSED GDGNAVAYPD TCVGTDSHTT MINGLGVLGW GVGGIEAEAA
MLGQPISMLI PEVVGFKLTG AMAEGVTATD LVLTCVQMLR EVGVVGRFVE FYGEGVANLT
LADRATIANM APEYGATCGF FGIDDKTLEY MRLTGRDEET IALVEAYSKE QGMWFTPENE
PVFTKTLELD ISKVVPSLAG PKRPQDRVAL PQVDELFNTD LKSIYSKDAP LRVDVDGKDH
DVGDGDVVIA AITSCTNTSN PDVLIAAGLV AKKAREKGLA PKPWVKTSLA PGSQVVTDYL
EKSGLQDDLD AMGFDLVGYG CTTCIGNSGP LAPPISKAIN GNDIVAASVL SGNRNFEGRV
SPDVRANFLA SPPLVVAYSI LGTVTQDITE TPLGKDQEGN DVMLADVWPT NAEIAEHRAA
NIDRQMFETR YADVYKGDEH WQAIKVEASD TYRWNPTSTY VASPPFFEGM EMTPAPVTDI
TDAKPLAILG DSVTTDHISP AGSIKEDSPA GSYLQSHQVA KQDFNSYGSR RGNHDVMMRG
TFANIRIKNE MVPGVEGGYT TYKGEQMPIY DAAMKHKEDG TPLVVVAGKE YGTGSSRDWA
AKGTILLGVK AVIVESFERI HRSNLIGMGV LPLQFKDGDT RNSLGLTATD SFTIKGLADL
TPSQDVEVEV TREDGSSFTF TALCRIDTAN EMEYYRNGGI LHYVLRKLAA A
//
