ID A6VWH6_MARMS Unreviewed; 914 AA.
AC A6VWH6;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 100.
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 OrderedLocusNames=Mmwyl1_1881 {ECO:0000313|EMBL:ABR70805.1};
OS Marinomonas sp. (strain MWYL1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=400668 {ECO:0000313|EMBL:ABR70805.1};
RN [1] {ECO:0000313|EMBL:ABR70805.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MWYL1 {ECO:0000313|EMBL:ABR70805.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Johnston A.W.B., Todd J.D., Rogers R., Wexler M., Bond P.L., Li Y.,
RA Richardson P.;
RT "Complete sequence of Marinomonas sp. MWYL1.";
RL Submitted (JUN-2007) 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; CP000749; ABR70805.1; -; Genomic_DNA.
DR AlphaFoldDB; A6VWH6; -.
DR STRING; 400668.Mmwyl1_1881; -.
DR KEGG; mmw:Mmwyl1_1881; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_013476_2_1_6; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
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; 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 67..586
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 716..843
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
FT REGION 399..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 914 AA; 99795 MW; 0A775E36B7AFC372 CRC64;
MNNSFDTQQQ ITVNGEQFHI HSLKGLGDKA KRLPFSLKIL LENLLRNEDG VNIKEQDIQA
LLNWDPQAKP ASEVAFTPAR VVMQDFTGVP AIVDLAAMRD AMEKLGGDPA KINPLSPAEL
VIDHSVQVDG YGNAAAFDLN TKLEYERNKE RYEFLRWGQT AFNNLKVVPP ATGIVHQVNL
EYLARVVFND DKNGQKFAYP DTLVGTDSHT TMINGLGVLG WGVGGIEAEA AMLGQPISLL
IPQVVGVKLS GRLPEGTTAT DLVLTITEML RNHGVVGKFV EFYGDGLADL PLADRATIAN
MAPEYGATCG IFPIDDETIN YLRLTNRDET QLNLIEEYAK HQGLWRNDGD EANYTDKLEL
ILNDVVPSLA GPKRPQDRIP LDKAGDTIRD HLKGFQDERM ARENKSSEEQ ARIESEGPVI
HPDESVDEAP IKGASIVKFK GQEFELNDGA CVIAAITSCT NTSNPSVILA AGLVAKKAKQ
LGINVKPWVK TSLAPGSKVV TDYLAKAGLM DDLESLGFNL VGYGCTTCIG NSGPLASEIS
DAIQKHKLIV SSILSGNRNF EGRIHQDVKM NFLASPPLVV AYAIAGRTDI DVYKEPLAQD
ANGNDIYLKD IWPSVKEVSD LVKETVTKEM FAKSYANVYE GDSHWQQIQI PDGKLYDWND
ASTYIKKATF FDGMSIDPPG IPSIKGARCL AKLGDSVTTD HISPAGSIKA DSPAGLYLQK
HGVEKAQFNS YGSRRGNHEV MVRGTFANVR LKNLLAPGTE GGITRTQPDD NLASIYDAAV
TYHESNTPLI ILAGKEYGTG SSRDWAAKGS LLLGVKAVIA ESYERIHRSN LIGMGVLPLQ
FKDGESYESL GLTGQEQFDI NGLQDKTDEV TLIATNSKGL KISFSADVRI DTPKEWDYYK
HGGILQYVLR GMLN
//
