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Database: UniProt
Entry: H5UUL9_9MICO
LinkDB: H5UUL9_9MICO
Original site: H5UUL9_9MICO 
ID   H5UUL9_9MICO            Unreviewed;       934 AA.
AC   H5UUL9;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 53.
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=acn {ECO:0000313|EMBL:GAB49427.1};
GN   ORFNames=MOPEL_130_00340 {ECO:0000313|EMBL:GAB49427.1};
OS   Mobilicoccus pelagius NBRC 104925.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermatophilaceae;
OC   Mobilicoccus.
OX   NCBI_TaxID=1089455 {ECO:0000313|EMBL:GAB49427.1, ECO:0000313|Proteomes:UP000004367};
RN   [1] {ECO:0000313|EMBL:GAB49427.1, ECO:0000313|Proteomes:UP000004367}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 104925 {ECO:0000313|EMBL:GAB49427.1,
RC   ECO:0000313|Proteomes:UP000004367};
RA   Yoshida Y., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA   Fujita N.;
RT   "Whole genome shotgun sequence of Mobilicoccus pelagius NBRC 104925.";
RL   Submitted (FEB-2012) 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}.
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:GAB49427.1}.
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DR   EMBL; BAFE01000089; GAB49427.1; -; Genomic_DNA.
DR   RefSeq; WP_009483270.1; NZ_BAFE01000089.1.
DR   AlphaFoldDB; H5UUL9; -.
DR   STRING; 1089455.MOPEL_130_00340; -.
DR   eggNOG; COG1048; Bacteria.
DR   UniPathway; UPA00223; UER00718.
DR   UniPathway; UPA00946; -.
DR   Proteomes; UP000004367; 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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004367}.
FT   DOMAIN          64..599
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          729..857
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   934 AA;  101762 MW;  9C8C8FF20D3A6E01 CRC64;
     MSQDSFQAKD TLEVRGKKYD IFRIDKVEGS KTLPYSLKVL LENLLRTEDG ANITADHIRA
     IGNWDENAQP DTEIQFTPAR VIMQDFTGVP CIVDLATMRE AAADLGGDPE RINPLSPAEL
     VIDHSVQIDV FGRRDAFERN VEYEYDRNGE RYQFLRWGQG AFDDFKVVPP GTGIVHQVNI
     EHLARVVMER DGVAYPDTCI GTDSHTTMEN GLGVLGWGVG GIEAEAAMLG QPVSMLIPRV
     VGFRVTGEIP AGVTATDVVL TITQMLRQHG VVGKFVEFHG EGVASIPLAN RATIGNMSPE
     FGSTCAIFPI DDKTIDYLRL TGRSDEQVAL VEAYTKEQGM WLDPSAQIRF SEQLELDLST
     VVPSIAGPKR PQDRILLSES KAQFAADLKN YVIDGNGIDK SSVDTELMES FPASDAPSHD
     VFDVSEADGA PVLSPPLRKG IDRATNPVTV TRDGQSFEID HGIVSIASIT SCTNTSNPSV
     MLAAGLLAKN AVEKGLKVKP WVKTSMAPGS KVVTEYYEKA GLWPALENLG YHLVGYGCTT
     CIGNSGPLPE EISAAINEND LAVTSVLSGN RNFEGRINPD VKMNYLASPP LVIAYALAGT
     MDFDFENEPL GQDSEGNDVF LRDIWPSSED VQSTIENSID RDMFTSQYAD VFAGDERWQG
     LDTPSGNTFE WDAQSTYVRK PPYFEGMTME LTPVNDISGA RVLARLGDSV TTDHISPAGA
     IKPDSPAGTY LAENGVDRKD FNSYGSRRGN HEVMIRGTFA NIRLKNQLLD GVEGGFTRDF
     TNGGEQSTIY DASVNYQEAG IPLVVLAGKE YGSGSSRDWA AKGTRLLGVK AVVAESYERI
     HRSNLIGMGV LPLQFPQGEN AESLGLDGTE TFDISGITEL NEGRTPKTVK VTATKDGGEQ
     VEFDAVVRID TPGEREYYLN DGILQYVLRS LVEH
//
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