ID A0A0M2LYS1_9MICO Unreviewed; 890 AA.
AC A0A0M2LYS1;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, 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:KKI20814.1};
GN ORFNames=XM48_06970 {ECO:0000313|EMBL:KKI20814.1};
OS Leucobacter sp. Ag1.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leucobacter.
OX NCBI_TaxID=1642040 {ECO:0000313|EMBL:KKI20814.1, ECO:0000313|Proteomes:UP000033836};
RN [1] {ECO:0000313|EMBL:KKI20814.1, ECO:0000313|Proteomes:UP000033836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ag1 {ECO:0000313|EMBL:KKI20814.1,
RC ECO:0000313|Proteomes:UP000033836};
RA Pei D., Kukutla P., Yu W., Xu J.;
RT "Draft Genome Sequences of Leucobacter sp. Ag1 from Mosquito Anopheles
RT gambiae.";
RL Submitted (APR-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:KKI20814.1}.
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DR EMBL; LAYO01000089; KKI20814.1; -; Genomic_DNA.
DR RefSeq; WP_046455077.1; NZ_LAYO01000089.1.
DR AlphaFoldDB; A0A0M2LYS1; -.
DR STRING; 1642040.XM48_06970; -.
DR PATRIC; fig|1642040.3.peg.2768; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000033836; 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; 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, ECO:0000313|EMBL:KKI20814.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000033836}.
FT DOMAIN 66..555
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 685..814
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 890 AA; 96100 MW; 5615BC652B77D783 CRC64;
MAAVNSFGAQ STLTVGGTDY QIYRIDKVPG HERLPYSLKV LLENLLRTED GANVTKQHVE
ALGSWDPNAQ PDTEIQFTPA RVIMQDFTGV PCIVDLATMR EAMADLGGDP QRINPLAPAE
LVIDHSVISD VYGSAGAFDK NVEIEYQRNG ERYQFLRWGQ GAFDDFKVVP PGTGIVHQVN
IEYLARVTFT REIDGVLNAY PDTCVGTDSH TTMENGLGVL GWGVGGIEAE AAMLGQPISM
LIPRVVGFKL SGQIPAGVTA TDVVLTITQM LRKHGVVGKF VEFYGEGVGS VPLANRATIG
NMSPEFGSTA AIFPIDDVTL DYLRLTGRPD DQIDLVKAYA QTQGMWHDPA HEPEFSEYLE
LDLSTVVASI AGPKRPQDRI ELTSAKGQFE RDLQNYAQAA NPAKVKDANG AEYTIDHGAV
TLASITSCTN TSNPSVMLAA GVLARNANAR GLKAKPWVKT TLAPGSKVVT DYYEKSGLTS
HLEDLGFYLV GYGCVTCIGN SGPLNEEVSA AVNENDLAVT AVLSGNRNFE GRINPDIKMN
YLASPPLVIA YALAGSMDFD FENEPLGQDA DGNDVYLREI WPDPVEVQKI ADSSIDSGMF
TEKYASVFDG DQRWTSLPTP DGDVFEWDAK STYVRKPPYF DGMPATPAPV SDISGARVLA
KLGDSVTTDH ISPAGNIKAE TPAGKYLQEN GIAPRDFNSY GSRRGNHEVM IRGTFANIRL
RNQLLDNVEG GFTRDFTQEG APQSYIYDAS QNYQAAGIPL VVLGGKEYGS GSSRDWAAKG
TSLLGVKAVI TESFERIHRS NLIGMGVLPL QFPAGENADS LGLDGTESFD ISGVTELNEG
RTPRTVHVTA THENGTVTEF DAVVRIDTPG EADYYRNGGI LQYVLRSLAA
//
