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
//