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Database: UniProt
Entry: A0A0P7ZJK2_9GAMM
LinkDB: A0A0P7ZJK2_9GAMM
Original site: A0A0P7ZJK2_9GAMM 
ID   A0A0P7ZJK2_9GAMM        Unreviewed;       904 AA.
AC   A0A0P7ZJK2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
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=acnA {ECO:0000313|EMBL:KPQ04283.1};
GN   ORFNames=HLUCCO02_04745 {ECO:0000313|EMBL:KPQ04283.1};
OS   Idiomarinaceae bacterium HL-53.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae.
OX   NCBI_TaxID=1298881 {ECO:0000313|EMBL:KPQ04283.1, ECO:0000313|Proteomes:UP000053932};
RN   [1] {ECO:0000313|EMBL:KPQ04283.1, ECO:0000313|Proteomes:UP000053932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HL-53 {ECO:0000313|EMBL:KPQ04283.1};
RA   Nelson W.C., Romine M.F., Lindemann S.R.;
RT   "Identification and resolution of microdiversity through metagenomic
RT   sequencing of parallel consortia.";
RL   Submitted (AUG-2015) 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}.
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:KPQ04283.1}.
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DR   EMBL; LIHO01000009; KPQ04283.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P7ZJK2; -.
DR   STRING; 1298881.Ga0003345_2313; -.
DR   PATRIC; fig|1298881.4.peg.909; -.
DR   OrthoDB; 9764318at2; -.
DR   UniPathway; UPA00223; UER00718.
DR   Proteomes; UP000053932; 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; CITRATE HYDRO-LYASE; 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|ARBA:ARBA00022485, 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|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU361275};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          74..574
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          703..830
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   904 AA;  98595 MW;  4727BDCBEA5F5543 CRC64;
     MASQDSFNTA SILDVAGKTL HYYSLPKAAE TLGNIDKLPV SLKVLLENLL RHEDGTTVTK
     EDIQAVADWL QTKSSKQEIE YRPARVLMQD FTGVPAVVDL AAMRDAVAKA GLPANRINPL
     SAVDLVIDHS VMVDKFASDE AFAENVKIEM ERNKERYEFL RWGQKAFNNF RVVPPGTGIC
     HQVNLEYLAK VAWTSEVDGK TYVYPDTLVG TDSHTTMING LGVLGWGVGG IEAEAAMLGQ
     PISMLIPEVI GFKLEGALPE GVTATDLVLT VTQMLRKKGV VGKFVEFYGP GLKHLPLADR
     ATIANMAPEY GATCGFFPVD EETLTYLKLS GRDEDVIERV EAYSKAQGMW RDDENEPVFT
     DTLTLNMKEV EPSLAGPKRP QDRVSLPQLR ESFDLLLKST SVSIDDEMGG LESISKAELG
     DSTAVPIAGT EHKLAHGDVV IAAITSCTNT SNPSVMLAAG LVAKKAVERG LQRKPWVKSS
     LAPGSKVVTD YLQAAGLEQY LDELGFDLVG YGCTTCIGNS GPLPDDVSQA IDKGDLVVSS
     VLSGNRNFEG RIHPQVKANW LASPPLVVAF ALAGTTRIDL SNDVIGEDKN GDPVYLKDIW
     PSSKEVQEAV QSVTSAMFKT QYAEVFDGDE HWQSLEIPDS ETYAWRDEST YVANPPFFEG
     IDKPAPKPTD IEGARVLAVF GDTITTDHIS PAGAIKGDSP AGKYLQAQGV AVKDFNSYGS
     RRGNHEVMMR GTFANIRIKN MMMDGREGGF TRYMPNDEEM SIYDAAMKYQ KENVPLVVLA
     GKEYGTGSSR DWAAKGTRLL GVKAVIAESY ERIHRSNLVG MGVLPLQFAE GESAQSLKLT
     GEEVISIHGL SENIKPGQKL KARAERKDGS FAEFEVLCRI DTANEVRYFL SGGILHYVLR
     QLVE
//
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