ID H0R4J2_9ACTN Unreviewed; 931 AA.
AC H0R4J2;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
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=acn {ECO:0000313|EMBL:GAB19993.1};
GN ORFNames=GOEFS_105_00040 {ECO:0000313|EMBL:GAB19993.1};
OS Gordonia effusa NBRC 100432.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1077974 {ECO:0000313|EMBL:GAB19993.1, ECO:0000313|Proteomes:UP000035034};
RN [1] {ECO:0000313|EMBL:GAB19993.1, ECO:0000313|Proteomes:UP000035034}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 100432 {ECO:0000313|EMBL:GAB19993.1,
RC ECO:0000313|Proteomes:UP000035034};
RA Yoshida I., Takarada H., Hosoyama A., Tsuchikane K., Katsumata H.,
RA Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Gordonia effusa NBRC 100432.";
RL Submitted (DEC-2011) 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 -!- 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:GAB19993.1}.
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DR EMBL; BAEH01000105; GAB19993.1; -; Genomic_DNA.
DR AlphaFoldDB; H0R4J2; -.
DR STRING; 1077974.GOEFS_105_00040; -.
DR eggNOG; COG1048; Bacteria.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000035034; Unassembled WGS sequence.
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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000035034}.
FT DOMAIN 71..595
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 724..854
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 931 AA; 101041 MW; 0780424C8807847F CRC64;
MSNDSFGARG TLEVGDNSYE IFRLNAVPGT EKLPYSLKVL AENLLRTEDG ANITKEHIEA
IANWDPSADP SIEIQFTPAR VIMQDFTGVP CVVDLATMRE AVTALGGDPN KVNPLSPAEM
VIDHSVILDV FGTADAFERN VELEYQRNAE RYQFLRWGQG AFDDFKVVPP GTGIVHQVNI
EYLARTVMVR NGQAYPDTCV GTDSHTTMEN GLGVLGWGVG GIEAEAAMLG QPVSMLIPRV
VGFKLTGEIN PGVTATDVVL TVTDMLRQHG VVGKFVEFYG NGVAEVPLAN RATLGNMSPE
FGSTCAIFPI DGETINYLRL TGRDDEQLAL VEAYAKEQGM WHAPENEPHF SEYLELDLST
VVPSIAGPKR PQDRILLSES KVAFRKDIHN YVEEQHPAAH TQLDEAVEES FPASDPVALS
FADDGAVKVQ SAANGSEGRP SKPVRVTGER GEFILDHGAV AVAGITSCTN TSNPSVMIGA
ALLARNAVEK GLSSKPWVKT NMAPGSQVVT DYYEKAGLWP YLEKLGFYLG GYGCTTCIGN
TGPLPDEISK AVNDNDLTVT AVLSGNRNFE GRISPDVKMN YLASPPLVIA YALAGTMDFD
FETDSLGKDN DGNDVFLKDI WPSPQEIDDT IKSAISQDMF RKSYADVFKG DENWRNLSTP
DGDTFEWSDD STYVRKAPYF DGMTLETTPV TDIKGARVLA KLGDSVTTDH ISPAGPIKPG
TPAAQYLDSH GVARKDYNSL GSRRGNHEVM IRGTFANIRL RNQLLDDVSG GYTRDFTQEG
GPQSFIYDAS QNYQKAGIPL VVLGGKEYGS GSSRDWAAKG TVLLGVKAVI TESFERIHRS
NLIGMGVVPL QFPEGESADS LKLTGTETFD ITGIEELNNG TIPETVHVTA TKEDGSVVEF
DAKVRIDTPG EADYYRNGGI LQYVLRNMLK S
//
