ID A0A0V8HWN1_9MICC Unreviewed; 902 AA.
AC A0A0V8HWN1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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:KSU66935.1};
GN ORFNames=AS038_03875 {ECO:0000313|EMBL:KSU66935.1};
OS Arthrobacter sp. NIO-1057.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=993071 {ECO:0000313|EMBL:KSU66935.1, ECO:0000313|Proteomes:UP000054434};
RN [1] {ECO:0000313|EMBL:KSU66935.1, ECO:0000313|Proteomes:UP000054434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIO-1057 {ECO:0000313|EMBL:KSU66935.1,
RC ECO:0000313|Proteomes:UP000054434};
RA Dastager S.G., Mawlankar R.B., Thorat M.N., Jiao J.-Y., Sonalkar V.,
RA Li W.-J.;
RT "Arthrobacter sp NIO-1057.";
RL Submitted (NOV-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=(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 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 -!- 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, 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:KSU66935.1}.
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DR EMBL; LNQJ01000002; KSU66935.1; -; Genomic_DNA.
DR RefSeq; WP_058254618.1; NZ_KQ758454.1.
DR AlphaFoldDB; A0A0V8HWN1; -.
DR STRING; 993071.AS038_03875; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000054434; Unassembled WGS sequence.
DR GO; GO:0047456; F:2-methylisocitrate dehydratase activity; IEA:UniProtKB-EC.
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; 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.
DR PROSITE; PS01244; ACONITASE_2; 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, ECO:0000313|EMBL:KSU66935.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 65..565
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 695..824
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 902 AA; 97500 MW; 858A89FBE7852FF9 CRC64;
MSNVDSFGAK GVLDVNGTEY EIYRLNKVEG SESLPYSLKV LLENLLRTED GANVTSDHIN
ALGQWDASAQ PNTEIQFTPA RVIMQDFTGV PCVVDLATMR EAVKDLGGDP TRVNPLAPAE
MVIDHSVQID TFGFEGAVER NMEIEYQRNG ERYQFLRWGQ TAFDDFKVVP PGTGIVHQVN
IEYLARTVMT REVNGVLRAY PDTCVGTDSH TTMVNGLGVL GWGVGGIEAE AAMLGQPVSM
LIPRVVGFKL AGSIPAGATA TDVVLTITEM LRKHGVVGKF VEFYGEGVAA VPLANRATIG
NMSPEFGSTA AMFPIDDVTL DYLRLTGRSE ENVALVEAYA KEQGMWHDPN REIRFSEYLE
LDLSTVVPSI SGPKRPQDRI ELSSAKEQFR KDLHNYVSDS EDTQGAGRPS VAVEVTKEDG
TAFTLDHGLV SIASITSCTN TSNPSVMLAA AVLARNAADK GLTSKPWVKT SVAPGSKVVT
EYYEKSGLLP YLEKLGFFVV GYGCATCIGN SGPLDAEISE AIQANDLAAT AVLSGNRNFE
GRINPDVKMN YLASPPLVIA YALAGTMDFD FETDALGQDA EGNDVFLKDI WPSPVEVQEI
IDSSIDKDMF AKGYDGVFDG DDRWKALDTP EGDTFAWDEK STYARKAPYF EGMTAEPQPV
QDIDGARVLL KLGDSVTTDH ISPAGSFKSE TPAGRYLIEN GVDRKDFNSY GSRRGNHEVM
IRGTFANIRI KNQLLDGVEG GFTRDFTQEG APQAYVYDAA ENYKAAGTPL VVLGGKEYGS
GSSRDWAAKG TALLGVKAVI TESFERIHRS NLIGMGVLPL QFPEGENADS LGLTGTETFA
VSGVTELNNG VTPKTLKVTA TAEDGKVTEF DAVLRIDTPG EADYYRNGGI LQYVLRQIAA
AN
//
