ID A0A0M2CR33_9MICC Unreviewed; 941 AA.
AC A0A0M2CR33;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
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:EYT48809.1};
GN ORFNames=H488_0115540 {ECO:0000313|EMBL:EYT48809.1};
OS Kocuria sp. UCD-OTCP.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Kocuria.
OX NCBI_TaxID=1292021 {ECO:0000313|EMBL:EYT48809.1, ECO:0000313|Proteomes:UP000033173};
RN [1] {ECO:0000313|EMBL:EYT48809.1, ECO:0000313|Proteomes:UP000033173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCD-OTCP {ECO:0000313|EMBL:EYT48809.1,
RC ECO:0000313|Proteomes:UP000033173};
RX PubMed=23661474;
RA Coil D.A., Doctor J.I., Lang J.M., Darling A.E., Eisen J.A.;
RT "Draft Genome Sequence of Kocuria sp. Strain UCD-OTCP (Phylum
RT Actinobacteria).";
RL Genome Announc. 1:E00172-13(2013).
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}.
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:EYT48809.1}.
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DR EMBL; AOSQ01000037; EYT48809.1; -; Genomic_DNA.
DR RefSeq; WP_017834182.1; NZ_AOSQ01000037.1.
DR AlphaFoldDB; A0A0M2CR33; -.
DR HOGENOM; CLU_013476_2_1_11; -.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000033173; 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; 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:EYT48809.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 72..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..455
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 941 AA; 102093 MW; 8DBBA80642DD1677 CRC64;
MSTVDSFGAK GVLDVKGTEY EIFRLNTLEG AQKLPYSLKV LLENLLRTED GANITSEHIE
ALANWDPTAE PSIEIQFTPG RVIMQDFTGV PCIVDLATMR EAIADLGGDP ARVNPLAPAE
LVIDHSVQID SFGTSDSIGI NMDIEYQRNG ERYQFLRWGQ TAFDDFKVVP PGMGIVHQVN
IENLARVVMT REVDGVLRAY PDTCVGTDSH TTMENGLGVL GWGVGGIEAE AAMLGQPISM
LIPRVVGFKL TGQIPSGATA TDVVLTITEM LREHGVVGKF VEFYGEGVGA VPLANRATIG
NMSPEFGSTA AIFPIDDVTL EYLRLTGRSD EQIDLVEAYV KEQGMWHDPS EEITFSEYLE
LDLSTVVPSI SGPKRPQDRI SLTDAKAQFH EDIKNYATHV DDNASGDTVD DVAAQSFPAS
DAPGYTADDH QSEADRPREH HAFAEDGRPS KQVPVTMPDG REFELDHGAV SIASITSCTN
TSNPSVMMAA AVLARNAVEK GLKAKPWVKT SIAPGSKVVT DYYEKSGLVP ALEELGFFIV
GYGCTTCIGN SGPLEDEISQ AIQDNDLAVT SVLSGNRNFE GRINPDVKMN YLASPPLVIA
YALAGNMDFD FESESLGQDA DGNEVYLKDI WPDPAEVQKI IDASIDTEMF TREYGTIFDG
DERWQNLDTP TGKTFEWNPE STYVRKPPYF EGMTMETTPV EDITGARVLL KLGDSVTTDH
ISPAGSFKSD TPAGKYLIEN GVQRKDFNSY GSRRGNHEVM IRGTFANIRI KNQLLDGVEG
GYTRDFTQEG GPQAAVYDAS INYQEAGVPL VVLGGKEYGS GSSRDWAAKG TSLLGVKAVI
AESYERIHRS NLIGMGVLPL QYPAGESADS LGLEGTETFD IQGVTGLNEG TTPKTLKVTA
TKEDGSTVEF DAVLRIDTPG EADYYRNGGI LQYVLRNIAK S
//
