ID A0A125QJZ5_9SPHN Unreviewed; 890 AA.
AC A0A125QJZ5;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=AUC45_11590 {ECO:0000313|EMBL:KWV92364.1};
OS Erythrobacter sp. YT30.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=1735012 {ECO:0000313|EMBL:KWV92364.1, ECO:0000313|Proteomes:UP000055668};
RN [1] {ECO:0000313|EMBL:KWV92364.1, ECO:0000313|Proteomes:UP000055668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YT30 {ECO:0000313|EMBL:KWV92364.1,
RC ECO:0000313|Proteomes:UP000055668};
RA Lin W., Zheng Q.;
RT "Draft genome sequence of Erythrobacter sp. YT30.";
RL Submitted (OCT-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:KWV92364.1}.
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DR EMBL; LMAF01000002; KWV92364.1; -; Genomic_DNA.
DR RefSeq; WP_067603852.1; NZ_LMAF01000002.1.
DR AlphaFoldDB; A0A125QJZ5; -.
DR STRING; 1735012.AUC45_11590; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000055668; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000055668}.
FT DOMAIN 72..562
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 692..816
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 890 AA; 96158 MW; 16F9E7A9331B2B6B CRC64;
MTAIGKDTLA TRSTLDVNGK QYAYYSLAKA SEQMGDVSKL PISMKVLLEN LLRFEDEGFT
VGKEHIQAIV DWQQNPKTGN EIQYRPARVL LQDFTGVPCV VDLAAMRDAI KELGGDTAKI
NPQVPVNLVI DHSVMVDEFG HPKAMEANMA LEYERNAERY DFLKWGSKSF ENFSAVPPGT
GICHQVNLEH IAQGIWSSAD ENGEMVAYPD TCVGTDSHTT MINGLGVLGW GVGGIEAEAA
MLGQPISMLI PEVVGFKLTG KMAEGVTATD LVLTCVQMLR EVGVVGRFVE FYGEGVANLT
LADRATIANM APEYGATCGF FGIDDKTIDY LRLTGRSEEN IALVEAYAKE QGMWFDPAHE
PVFSNTLELD VASVVPSLAG PKRPQDRVIL PEVDELFNGD LAKVYKKEAP VRTAVEGKDH
DIGDGDVVIA AITSCTNTSN PDVLIAAGLV AKKANERGMQ PKPWVKTSLA PGSQVVTDYL
VKSGLQDDLD AIGFDLVGYG CTTCIGNSGP LAPPISKAIN GNDIVAASVL SGNRNFEGRV
SQDVRANFLA SPPLVVAYAL KGTVTEDITT TPLGQDKEGN DVMLADLWPS NAEIAEHRAA
NIDRSMFESR YANVYDGDEH WQAITVEPSD TYQWRAGSTY VANPPYFEGM GMEPAPVEDI
VNAKPLAVLG DSVTTDHISP AGAIKEDSPA GEYLKSNQVA KKDFNSYGSR RGNHDVMMRG
TFANIRIKNE MVPGVEGGVT TYNGEQMPIY DAAMKHKADG TPLIVVGGKE YGTGSSRDWA
AKGTILLGVR AVIVESFERI HRSNLVGMGV LPLQFTGGDT RETLNLDADC TFCIKGLADL
TPGQQLEIDV TRGDGTSFTF TALCRIDTAN EMEYYRNGGI LHYVLRKLAA
//
