ID A0A0Q5ULG7_9SPHN Unreviewed; 894 AA.
AC A0A0Q5ULG7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=ASG20_09770 {ECO:0000313|EMBL:KQS49305.1};
OS Sphingomonas sp. Leaf198.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736299 {ECO:0000313|EMBL:KQS49305.1, ECO:0000313|Proteomes:UP000050871};
RN [1] {ECO:0000313|Proteomes:UP000050871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf198 {ECO:0000313|Proteomes:UP000050871};
RA Garrido-Oter R.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000050871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf198 {ECO:0000313|Proteomes:UP000050871};
RA Vorholt J.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
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:KQS49305.1}.
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DR EMBL; LMPX01000002; KQS49305.1; -; Genomic_DNA.
DR RefSeq; WP_056051495.1; NZ_LMPX01000002.1.
DR AlphaFoldDB; A0A0Q5ULG7; -.
DR STRING; 1736299.ASG20_09770; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000050871; 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:UP000050871}.
FT DOMAIN 71..566
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 696..821
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 894 AA; 96866 MW; 48B4010A37A4C2EE CRC64;
MTAIGQDTLK TRTSLSTGGK SYDYYSLAKA SEQLGDISRL PFSMKVLLEN LLRFEDGVTV
TREDIQAIVD WQKERRSDRE IQYRPARVLM QDFTGVPCVV DLAAMRDAMT KLGGNPEKIN
PQVPVHLVID HSVMVDEFGT PQAFHDNVDL EYERNIERYE FLKWGSKALD NFQVVPPGTG
ICHQVNLEYI GQAVWSSASS GDHGDGTMIA YPDTLVGTDS HTTMINGLGV LGWGVGGIEA
EAAMLGQPVS MLIPEVVGFK LLGKLNEGIT ATDLVLTVTQ MLRAKGVVGR FVEFFGPGLS
SMTLADRATI ANMAPEYGAT CGFFPIDDKT LDYMRLTARS DENVELVEAY AKANGFWRDE
NAEDPVFTDT LELDMGTVVA SLAGPKRPQD RVSLNKVDEV FNSDLHKLYH KEQPARVAVE
GREHDIGDGD VVIAAITSCT NTSNPSVLVA AGLVARKANA LGLKSKPWVK TSLAPGSQVV
TDYLDKAGLT ADLNALGFNL VGYGCTTCIG NSGPLAPAIS AAINENDLVA ASVLSGNRNF
EGRVSPDVRA NFLASPPLVV AYAIKGTVTT DMIETPLGQG SDGQDVYLRD IWPTNEEVRT
TMDANIDAGM FGARYGDVYA GDAKWREIDV TGSDTYAWRA GSTYVANPPY FEGLSMTPSP
VQDIIDAKPL AILGDSITTD HISPAGSIKA DSPAGRFLQE HQVSKADFNS YGARRGNHDV
MMRGTFANIR IKNEMVPGIE GGMSKYDGEV MAIYDAAMRF KQDGTPLVIV AGKEYGTGSS
RDWAAKGTNL LGVRAVITES FERIHRSNLV GMGVLPLQFA EGTDRKTLGL DGSETFTILD
VASIRPRQDV TVKMTRADGS SETFQTKCRI DTVNELEYFL NGGILHYVLR KLAA
//
