ID A0A074MSC5_ERYLO Unreviewed; 890 AA.
AC A0A074MSC5;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=EH31_16365 {ECO:0000313|EMBL:KEO88532.1};
OS Erythrobacter longus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=1044 {ECO:0000313|EMBL:KEO88532.1, ECO:0000313|Proteomes:UP000027647};
RN [1] {ECO:0000313|EMBL:KEO88532.1, ECO:0000313|Proteomes:UP000027647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6997 {ECO:0000313|EMBL:KEO88532.1,
RC ECO:0000313|Proteomes:UP000027647};
RA Zheng Q.;
RT "A comprehensive comparison of genomes of Erythrobacter spp. strains.";
RL Submitted (APR-2014) 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:KEO88532.1}.
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DR EMBL; JMIW01000009; KEO88532.1; -; Genomic_DNA.
DR RefSeq; WP_034962060.1; NZ_JMIW01000009.1.
DR AlphaFoldDB; A0A074MSC5; -.
DR STRING; 1044.EH31_16365; -.
DR eggNOG; COG1048; Bacteria.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000027647; 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:UP000027647}.
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..817
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 890 AA; 95984 MW; 0519DCAE87622AC9 CRC64;
MTATGKDSLS ARSTLEVNGK SYAYYSLDKA AEQMGDVSKL PISMKVLLEN MLRFEDGGFT
VGREDIQAII DWQKNPVTGS EIQYRPARVL LQDFTGVPCV VDLAAMRDAI KKLGGDTAKI
NPQVPVDLVI DHSVMVDEFG HPKAMEANMA LEYERNAERY DFLKWGSKSF ENFTAVPPGT
GICHQVNLEY IGRGVWSSED ANGDLVAYPD TCVGTDSHTT MINGLGVLGW GVGGIEAEAA
MLGQPISMLI PEVVGFKLTG RMAEGVTATD LVLTCVEMLR KVGVVGSFVE FYGEGVANLT
LADRATIANM APEYGATCGF FGIDHKTIDY MRLTGRSEDT IALVEAYAKA QGMWFDPTNE
PVFSNTLELD VGTVVPSLAG PKRPQDRVTL GQVDELFNED LAKVYKKTQA ARVDVADTDH
DIGDGDVVIA AITSCTNTSN PDVLIAAGLV AKKANERGMR PKPWVKTSLA PGSQVVTDYL
VKSGLQDDLD ALGFDLVGYG CTTCIGNSGP LAPPISDAIN GNDIVAASVL SGNRNFEGRV
SPDVRANFLA SPPLVVAYAL KGTVTEDIIE TPIGQDQDGN DVMLADLWPS NAEIAEHRAA
NIDRSMFVKR YANVFDGDEH WQAITVEPSD TYQWRAGSTY IANPPYFEGM EMTPAPITDI
VDAKPLAILG DSVTTDHISP AGAIKEDSPA GAYLKGNQVA KKDFNSYGSR RGNHDVMMRG
TFANIRIKNE MVPGIEGGVT TYNGEQMPIY DAAMRHKADG TQLIVVGGKE YGTGSSRDWA
AKGTILLGVR AVIVESFERI HRSNLVGMGV LPLQFKEGDT RASLGINADC TFSILGLADL
KPGQDVEVEA TRGDGSTFTF TALCRIDTEN EMEYYRNGGI LHYVLRKLAA
//
