ID A0A075JKM0_9MICO Unreviewed; 934 AA.
AC A0A075JKM0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
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:AIF40628.1};
GN ORFNames=HX89_06410 {ECO:0000313|EMBL:AIF40628.1};
OS Dermacoccus nishinomiyaensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermacoccaceae;
OC Dermacoccus.
OX NCBI_TaxID=1274 {ECO:0000313|EMBL:AIF40628.1, ECO:0000313|Proteomes:UP000027986};
RN [1] {ECO:0000313|EMBL:AIF40628.1, ECO:0000313|Proteomes:UP000027986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M25 {ECO:0000313|EMBL:AIF40628.1,
RC ECO:0000313|Proteomes:UP000027986};
RA Hong K.W., Chan K.G.;
RT "Genome Sequencing of Dermacoccus nishinomiyaensis.";
RL Submitted (JUL-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=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = 2-methyl-cis-
CC aconitate + H2O; Xref=Rhea:RHEA:17941, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57429, ChEBI:CHEBI:57872; EC=4.2.1.99;
CC Evidence={ECO:0000256|ARBA:ARBA00000118};
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 -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC {ECO:0000256|ARBA:ARBA00005026}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185, ECO:0000256|RuleBase:RU361275}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP008889; AIF40628.1; -; Genomic_DNA.
DR RefSeq; WP_038567856.1; NZ_CP008889.1.
DR AlphaFoldDB; A0A075JKM0; -.
DR GeneID; 41840801; -.
DR KEGG; dni:HX89_06410; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_013476_2_1_11; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000027986; Chromosome.
DR GO; GO:0047456; F:2-methylisocitrate dehydratase activity; IEA:UniProtKB-EC.
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; 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|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|RuleBase:RU361275, ECO:0000313|EMBL:AIF40628.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000027986}.
FT DOMAIN 66..597
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 727..855
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
FT REGION 392..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 934 AA; 100962 MW; 32498D56A9B45F29 CRC64;
MSQSTDSFGA KGSLEVGSNS YEIYRINTVE GSKNLPYSLK VLLENLLRTE DGANVTKEQI
AALGNWDENA DPDTEIQFTP ARVIMQDFTG VPCVVDLATM REAVGDLGGD PAKINPLAPA
EMVIDHSVII EDFGNPQAFE KNIEIEYQRN EERYQFLRWG QTAFNEFAVV PPDTGIVHQV
NIERLARTVM VREGKAYPDS CVGTDSHTTM VNGLGVLGWG VGGIEAEAAM LGQPVSMLIP
RVVGFKLTGS TKPGVTATDV VLTITEMLRK HGVVGKFVEF YGDGVAEVPL ANRATIGNMS
PEFGSTCAIF PIDDVTLDYL RLTGRDDEQV ALVEAYAKEQ GLWHDPSNEP RFSEYLELDL
GEVVPSIAGP KRPQDRIILS ESKKTFREQL PSYTSGVEGN GVEGTTFPAS DPVQPGSDEQ
ADNSTPVTPV EAAVPSAEGR VSKPVEVKMN DGRSFTLDHG HVAIASITSC TNTSNPSVMM
AAGLLAKKAA DKGLTRKPWV KTSMAPGSKV VTAYYDAAGL WESLEKVGFY LVGYGCATCI
GNSGPLEQEI SDAINANDIT ATAVLSGNRN FEGRISPDVK MNYLASPPLV IAYALAGTMD
FDFENDAIGK DDDGNDVFLK DIWPSAEEVD AAIKGAIKKD LFTKEYADVF AGDERWQSLQ
TPEGKTFAWD EKSTYVRKPN YFDGMKMETT PVTDIKGARV LAKLGDSVTT DHISPAGNIK
ADSPAGKYLA ERGVERKDFN SYGSRRGNHE VMVRGTFANI RLKNQLLDGV EGGFTRNFLN
GGEQTTIFEA SEAYQEAGVP LVVLGGKEYG SGSSRDWAAK GTRLLGVKAV IAESFERIHR
SNLIGMGVLP LQFPAGKTAD DLGLDGTETF EITGIEALNE GTTPKTVKVV ATKDGSEPIE
FDAVVRIDTP GEADYYRNDG ILQYVLRNLV KNAA
//
