ID A0A0U2XNT8_9MICC Unreviewed; 940 AA.
AC A0A0U2XNT8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Aconitate hydratase A {ECO:0000256|ARBA:ARBA00019378};
DE EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
DE EC=4.2.1.99 {ECO:0000256|ARBA:ARBA00013250};
DE AltName: Full=(2R,3S)-2-methylisocitrate dehydratase {ECO:0000256|ARBA:ARBA00031613};
DE AltName: Full=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate dehydratase {ECO:0000256|ARBA:ARBA00030846};
DE AltName: Full=Iron-responsive protein-like {ECO:0000256|ARBA:ARBA00031977};
DE AltName: Full=Probable 2-methyl-cis-aconitate hydratase {ECO:0000256|ARBA:ARBA00033025};
DE AltName: Full=RNA-binding protein {ECO:0000256|ARBA:ARBA00031081};
GN Name=acnA {ECO:0000313|EMBL:ALU39906.1};
GN ORFNames=AS188_09255 {ECO:0000313|EMBL:ALU39906.1}, KFL01_11230
GN {ECO:0000313|EMBL:GEO91817.1};
OS Kocuria flava.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Kocuria.
OX NCBI_TaxID=446860 {ECO:0000313|EMBL:ALU39906.1, ECO:0000313|Proteomes:UP000057181};
RN [1] {ECO:0000313|EMBL:ALU39906.1, ECO:0000313|Proteomes:UP000057181}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HO-9041 {ECO:0000313|EMBL:ALU39906.1,
RC ECO:0000313|Proteomes:UP000057181};
RA Zhou M., Dai J.;
RT "Complete Genome Sequence of Kocuria flava strain HO-9041.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GEO91817.1, ECO:0000313|Proteomes:UP000321155}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 107626 {ECO:0000313|EMBL:GEO91817.1,
RC ECO:0000313|Proteomes:UP000321155};
RA Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT "Whole genome shotgun sequence of Kocuria flava NBRC 107626.";
RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
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 -!- 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}.
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DR EMBL; CP013254; ALU39906.1; -; Genomic_DNA.
DR EMBL; BJZR01000022; GEO91817.1; -; Genomic_DNA.
DR RefSeq; WP_058858614.1; NZ_CP013254.1.
DR AlphaFoldDB; A0A0U2XNT8; -.
DR STRING; 446860.AS188_09255; -.
DR KEGG; kfv:AS188_09255; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000057181; Chromosome.
DR Proteomes; UP000321155; Unassembled WGS sequence.
DR GO; GO:0047456; F:2-methylisocitrate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
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 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 Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Lyase {ECO:0000313|EMBL:ALU39906.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000057181}.
FT DOMAIN 65..605
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 735..864
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
FT REGION 416..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..447
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 940 AA; 102081 MW; 1EC3CF5BF9C330C9 CRC64;
MSTVDSFGAK GVLDVDGTEY EIFRLNALEG AAKLPYSLKV LLENLLRTED GANITSEHIR
ALAEWDAEAE PSIEIQFTPG RVIMQDFTGV PCIVDLATMR EAVADLGGDP SRVNPLAPAE
LVIDHSVQID AFGTADAIER NMDIEYQRNG ERYQFLRWGQ TAFDDFKVVP PGMGIVHQVN
IENLARVVMT REVDGALRAY PDTCVGTDSH TTMENGLGVL GWGVGGIEAE AAMLGQPISM
LIPRVVGFKL TGEIPAGATA TDVVLTITEM LREHGVVGKF VEFYGEGVGA VPLANRATIG
NMSPEFGSTA AIFPIDDVTL EYLRLTGRSD EQVALVEAYV KEQGMWHDPS EEITFSEYLE
LDLSTVVPSI SGPKRPQDRI ALTEAKAQFH EDIKNYATHV DDAASGDTVD DVAAQSFPAS
DAPGYTADDH QSEADRPREH HAHAENGRPT KQVPVTMPDG REFELDHGAV SIASITSCTN
TSNPSVMMAA AVLARNAVEK GLKAKPWVKT SIAPGSKVVT NYYEKSGLVP ALEELGFYIV
GYGCTTCIGN SGPLEEEISQ AIQDNDLAVT SVLSGNRNFE GRINPDVKMN YLASPPLVIA
YALAGNMDFD FETEPLGQDA EGNDVYLKDI WPDPAEVQRI IDSSIDTEMF TREYGTIFDG
DERWQNLDTP TGKTFEWNEQ STYVRKPPYF EGMTMETTPV EDITGARVLL KLGDSVTTDH
ISPAGSFKSD TPAGKYLIEH GVERKDFNSY GSRRGNHEVM IRGTFANIRI KNQLLDGVEG
GFTRDFTRDG GPQETVYDAA MNYKEAGVPL VVLGGKEYGS GSSRDWAAKG TSLLGVKAVI
AQSYERIHRS NLIGMGVLPL QFPAGESAES LGLDGTESFD VQGVTALNEG TTPKTLKVVA
TKEDGATVEF DAVLRIDTPG EADYYRNGGI LQYVLRQIAK
//
