ID W9GUE2_9PROT Unreviewed; 902 AA.
AC W9GUE2;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=N825_17520 {ECO:0000313|EMBL:EWY37409.1};
OS Skermanella stibiiresistens SB22.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Skermanella.
OX NCBI_TaxID=1385369 {ECO:0000313|EMBL:EWY37409.1, ECO:0000313|Proteomes:UP000019486};
RN [1] {ECO:0000313|EMBL:EWY37409.1, ECO:0000313|Proteomes:UP000019486}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB22 {ECO:0000313|EMBL:EWY37409.1,
RC ECO:0000313|Proteomes:UP000019486};
RA Zhu W., Wang G.;
RT "The genome sequence of Skermanella stibiiresistens.";
RL Submitted (AUG-2013) 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:EWY37409.1}.
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DR EMBL; AVFL01000026; EWY37409.1; -; Genomic_DNA.
DR RefSeq; WP_037458822.1; NZ_AVFL01000026.1.
DR AlphaFoldDB; W9GUE2; -.
DR STRING; 1385369.N825_17520; -.
DR PATRIC; fig|1385369.3.peg.5479; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000019486; 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:UP000019486}.
FT DOMAIN 79..568
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 704..825
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 902 AA; 96908 MW; 1BCAAEF8F1054BDC CRC64;
MTTFTGHDTL KTRRTLDVGG KSYDYFSLKA AEQAGLGDVS TLPFSLKVLL ENLLRFEDGR
TVSVGDVKAL GQWLKDRKSD TEIAYRPARV LMQDFTGVPA VADLAAMREA VKSLGGEVSR
INPLCAVDLV IDHSVMVDEF GTGTAFKRNV DLEFERNQER YAFLRWGQTA FNNFRVVPPG
TGICHQVNVE YLAQTVWTDT DQATGKTIAY PDTLVGTDSH TTMVNGLAVL GWGVGGIEAE
AAMLGQPISM LIPEVVGFKL IGALKEGTTA TDLVLTVTQM LRKRGVVGKF VEFFGPGLAA
LPLADRSTIA NMAPEYGATC GIFPIDAETI KFLTFTGRDA ERVALVEAYA KAQGMWAEPG
SPEPVFTDVL ELDLSTVEPS LAGPKRPQDK VLLSAMSSTF TSDLTASFKV PTGDESKETP
VKGAGYSLKQ GDVVIAAITS CTNTSNPSVL VAAGLVAKKA VEKGLTSKPW VKTSLAPGSQ
VVTDYLAAAG LDTYLDKLGF NLVGYGCTTC IGNSGPLPEA ISAAVEEGDL VVAAVLSGNR
NFEGRVNPHT RANYLASPPL CVAYALAGNV KVDLVNDPIG MGSDGQPVFL KDIWPSNQEI
ADTIQASLTP AMFRQRYGNV FAGPPEWQSI ETATGDTYKW VDGSTYVKLP PLFEDMKPEP
EAVSDVHGAR SLAILGDSIT TDHISPAGSI KKTSPAGEYL MGYQVRPEDF NSYGARRGNH
EVMMRGTFAN IRIKNEMVPG TEGGVTKHIP SGEVLPIYTA AMRYADEGTP LVIIAGKEYG
TGSSRDWAAK GTRLLGVKAV LAESFERIHR SNLIGMGILA LQFKDGMTRQ SLKLDGTETF
DVTGVESGLT PRKDIDVRIT RADGSSETIK VMLRIDTLDE VEYYKNGGIL QYVLRSMMKS
AA
//
