ID C7JG48_ACEP3 Unreviewed; 897 AA.
AC C7JG48;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 83.
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 OrderedLocusNames=APA01_25120 {ECO:0000313|EMBL:BAI00618.1};
OS Acetobacter pasteurianus (strain NBRC 105184 / IFO 3283-01).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acetobacter.
OX NCBI_TaxID=634452 {ECO:0000313|EMBL:BAI00618.1, ECO:0000313|Proteomes:UP000000948};
RN [1] {ECO:0000313|EMBL:BAI00618.1, ECO:0000313|Proteomes:UP000000948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 105184 / IFO 3283-01 {ECO:0000313|Proteomes:UP000000948};
RX PubMed=19638423; DOI=10.1093/nar/gkp612;
RA Azuma Y., Hosoyama A., Matsutani M., Furuya N., Horikawa H., Harada T.,
RA Hirakawa H., Kuhara S., Matsushita K., Fujita N., Shirai M.;
RT "Whole-genome analyses reveal genetic instability of Acetobacter
RT pasteurianus.";
RL Nucleic Acids Res. 37:5768-5783(2009).
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}.
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DR EMBL; AP011121; BAI00618.1; -; Genomic_DNA.
DR RefSeq; WP_003624593.1; NC_013209.1.
DR AlphaFoldDB; C7JG48; -.
DR STRING; 634452.APA01_25120; -.
DR GeneID; 60375144; -.
DR KEGG; apt:APA01_25120; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_013476_2_1_5; -.
DR BioCyc; APAS634452:APA01_RS12760-MONOMER; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000000948; Chromosome.
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 78..564
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 695..822
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 897 AA; 97654 MW; 7AE6176D7E9EAD66 CRC64;
MKTVGHDKLK TGRTLEVDGK TYHYFSIPEA AKTIGDVSRL PVSLKVLLEN ILRFEDGRSY
NVEDAKAIAG WLPKGSSSKE VPFKPSRILM QDFTGVPGVV DLAAMRDGIV SLKGDPQKVN
PMVPVNLVID HSVMVDYAGT KDALQENITL EFERNAERYA FLRWGQEAFE NFSVVPPDTG
ICHQVNLEYI AQVAWTANVG GKEYVYPDSL YGTDSHTTMI NGLGVLGWGV GGIEAEAAML
GQPIAMLIPD VIGFKLTGKL PEGATATDLV LTVTQMLRKK GVVGKFVEFF GPALDHLPVA
DRSTIANMAP EYGATCGFFP VDALTLDFLR QTGRDEHRIK LVEEYLRAQG MFRTHETPEP
VFTDILELDL STVVPSLAGP KRPQDRVELK SAKTAFEKEL TSSLGVAAND ADKKVPVAGT
NYDLGQGDIV IAAITSCTNT SNPAVLIAAG LVARKARALG LKPKPWVKTS LAPGSQVVTD
YLNRSGLTTD LDAMGFNTVG YGCTTCIGNS GPLPSHIVDA IENNDLVAVS VLSGNRNFEG
RISPNVRANY LASPPLVVAY SLLGTMRQDI TTEQLGTSKD GKPVYLKDIW PSNKEIADLI
ASAISRDEFI SRYKDVSKGT KEWQGLKVAT GSETYKWDPK STYVQDPPYF KHMEVEPKAP
GNIEGARILA LLGDNITTDH ISPAGSIKKD SPAGRYLMEH GVEPKDFNSY GSRRGNDRVM
VRGTFANIRI KNEMLPGTEG GYSKHFPDGK EGAIYDVAME YKKEHTPLVV IGGKEYGMGS
SRDWAAKGTL LLGVKAVIAE SFERIHRSNL VGMGVLPLVF KDGTTRKTLG LKGDEVISIK
GVDKLSPRMD VIMTITRNDG STQEVPLLCR VDTLDEVEYY RHGGILQYVL RGMTKAA
//
