ID Q6NDA7_RHOPA Unreviewed; 905 AA.
AC Q6NDA7;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 120.
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 Name=acnA {ECO:0000313|EMBL:CAE25646.1};
GN OrderedLocusNames=RPA0202 {ECO:0000313|EMBL:CAE25646.1};
OS Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=258594 {ECO:0000313|EMBL:CAE25646.1, ECO:0000313|Proteomes:UP000001426};
RN [1] {ECO:0000313|EMBL:CAE25646.1, ECO:0000313|Proteomes:UP000001426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-98 / CGA009 {ECO:0000313|Proteomes:UP000001426};
RX PubMed=14704707; DOI=10.1038/nbt923;
RA Larimer F.W., Chain P., Hauser L., Lamerdin J., Malfatti S., Do L.,
RA Land M.L., Pelletier D.A., Beatty T.J., Lang A.S., Tabita F.R.,
RA Gibson J.L., Hanson T.E., Torres y Torres J., Peres C., Harrison F.H.,
RA Gibson J., Harwood C.S.;
RT "Complete genome sequence of the metabolically versatile photosynthetic
RT bacterium Rhodopseudomonas palustris.";
RL Nat. Biotechnol. 22:55-61(2004).
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; BX572593; CAE25646.1; -; Genomic_DNA.
DR RefSeq; WP_011155770.1; NZ_CP116810.1.
DR AlphaFoldDB; Q6NDA7; -.
DR STRING; 258594.RPA0202; -.
DR GeneID; 66891207; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_013476_2_1_5; -.
DR PhylomeDB; Q6NDA7; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000001426; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001426}.
FT DOMAIN 77..569
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 699..831
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 905 AA; 98544 MW; 1ED3A22C5E7C6AA0 CRC64;
MTSLDSFKCR KILKVGSKSY VYYSLPTAEK NGLKGISRLP YSMKVLLENL LRNEDDRTVK
KADIMAVAKW MRKKALEHEI AFRPARVLMQ DFTGVPAVVD LAAMRNAMQK LGGDAEKINP
LVPVDLVIDH SVIVNFFGNN QAFKKNVAEE YKQNQERYEF LKWGQKAFSN FAVVPPGTGI
CHQVNLEYLA QTVWTKKEKM TIGRKTGTFE VAYPDTLVGT DSHTTMVNGL AVLGWGVGGI
EAEAAMLGQP LSMLLPEVVG FKLKGALKEG VTATDLVLTV TQMLRKQGVV GKFVEFFGPG
LDNLSVADKA TIANMAPEYG ATCGFFPVDG ETIDYLKTSG RASARVALVE KYAKAQGLFR
TAKSPDPVFT VTLTLDLADV VPSLAGPKRP EGRVALPAVA EGFTTAMDAE YKKALDGARY
KVEGRNFDIG HGDVVIAAIT SCTNTSNPSV LIGAGLLARN AAAKGLKAAP WVKTSLAPGS
QVVAEYLANS GLQKDLDKVG FNLVGFGCTT CIGNSGPLPE EISKSINDNG IVAAAVLSGN
RNFEGRVSPD VQANYLASPP LVVAYALAGS VTKNLAVDPI GTGKDGKPVY LKDIWPSTKE
INAFVKKYVT SKIFKARYAD VFKGDTNWRK IKTVESETYK WNMSSTYVQN PPYFEGMTKQ
PEPITDVVDA RVLALFGDKI TTDHISPAGS IKLTSPAGKY LTERQVRPAD FNQYGTRRGN
HEVMMRGTFA NIRIKNHMLK GADGNIPEGG LTKHWPDGEQ MSIYDAAMKY QEEKVPLVVF
AGAEYGNGSS RDWAAKGTRL LGVRAVICQS FERIHRSNLV GMGVLPLTFE EGTSWASLGL
KGDEKVTIRG LEGDLKPRQM LEAEITSAAG KRKRVPLLCR IDTLDELDYY RNGGILHYVL
RKLAA
//
