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Database: UniProt
Entry: A0A1H3XAW5_9BACT
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ID   A0A1H3XAW5_9BACT        Unreviewed;       919 AA.
AC   A0A1H3XAW5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
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   ORFNames=SAMN05660909_00360 {ECO:0000313|EMBL:SDZ96433.1};
OS   Chitinophaga terrae (ex Kim and Jung 2007).
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=408074 {ECO:0000313|EMBL:SDZ96433.1, ECO:0000313|Proteomes:UP000199656};
RN   [1] {ECO:0000313|Proteomes:UP000199656}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23920 {ECO:0000313|Proteomes:UP000199656};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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=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   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC       {ECO:0000256|ARBA:ARBA00007185, ECO:0000256|RuleBase:RU361275}.
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DR   EMBL; FNRL01000001; SDZ96433.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H3XAW5; -.
DR   STRING; 408074.SAMN05660909_00360; -.
DR   OrthoDB; 9764318at2; -.
DR   UniPathway; UPA00223; UER00718.
DR   Proteomes; UP000199656; Unassembled WGS sequence.
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; 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   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.
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}.
FT   DOMAIN          57..576
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          706..832
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   919 AA;  101097 MW;  44145FAD5D611F11 CRC64;
     MEPKIALLSK LEQEGKQISR LPFSIRILLE NVLRNKDNFA ITDEHVETLV NWTPGGTDKE
     VPFKPARVLM QDFTGVPAVV DLASIRAEVI RQGKDGAAIN PAIPVDLVVD HSVQVDFFGT
     DYSYRKNVAY EYERNKERYQ LLKWAQQAFR NFTVVPPGMG ICHQVNLEYL AKGVISRDGW
     IFPDTLVGTD SHTPMVNGIG VLGWGVGGIE AEAAILGQPI YFTCPQVIGL KLTGKLTEGV
     TATDMVLAIT ELLRKYGVVD KFVEVFGDGL DHLTVPDRAT ISNMSPEFGC TVTYFPVDDQ
     TLQYMRRTNR PADQISLVES YCRQNMLWRN GDENITYSDI LELDLNKVQA AVAGPKRPQD
     RILVKDLGNE FETLLGKEYK RMYTPEGKRR DTAWLSEGGS GTTFTYEIQK PLEDVAVEVD
     YLKSVRVKLR NEEYVLSDGA ITIAAITSCT NTSNPSVMIG AGLVAKKAIS RGLTVKPWVK
     TSLAPGSRVV TDYLKRANLL EELEALRFHV VGYGCTSCIG NSGPLPPAIA EAVDKGNLVV
     ASVLSGNRNF EARVHPQVKM NFLASPMLVV AYAIVGRVDI DLLTAPLGYD PNGEPVYLRD
     IWPTQEEINQ AIATAVKQED FENAYSVIFD GDEQWQGLLA PTGNNYHWSN DSTYIREAPF
     FKGISSQLEP LHDITGARVL LKLGDSVTTD HISPAGSFKS DTPAGKYLLD HGIDQRMFNS
     YGSRRGNHEV MVRGTFANVR LKNDLSPKEG GYTTLMPSGT VLSVYDASVK YAASGTPLIV
     LAGKEYGSGS SRDWAAKGTN LLGVKAIIAE SYERIHRSNL VGMGILPLEY MNGQNAASLN
     LTGTEQYDIT GLEGGLTPGK VLKVKAIPGS GEPPVEFDVK CKLNSEIEIE YYLNGGILQY
     VLRDFLARGF TQNVSRREA
//
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