ID A0A1J4ZP33_9CHLR Unreviewed; 727 AA.
AC A0A1J4ZP33;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_01027, ECO:0000256|HAMAP-Rule:MF_01032};
DE Includes:
DE RecName: Full=3-isopropylmalate dehydratase large subunit {ECO:0000256|HAMAP-Rule:MF_01027};
DE EC=4.2.1.33 {ECO:0000256|HAMAP-Rule:MF_01027};
DE AltName: Full=Alpha-IPM isomerase {ECO:0000256|HAMAP-Rule:MF_01027};
DE Short=IPMI {ECO:0000256|HAMAP-Rule:MF_01027};
DE AltName: Full=Isopropylmalate isomerase {ECO:0000256|HAMAP-Rule:MF_01027};
DE Includes:
DE RecName: Full=3-isopropylmalate dehydratase small subunit {ECO:0000256|HAMAP-Rule:MF_01032};
GN Name=leuC {ECO:0000256|HAMAP-Rule:MF_01027};
GN Synonyms=leuD {ECO:0000256|HAMAP-Rule:MF_01032};
GN ORFNames=AUK03_16335 {ECO:0000313|EMBL:OIO88388.1};
OS Anaerolineae bacterium CG2_30_64_16.
OC Bacteria; Chloroflexota; Anaerolineae.
OX NCBI_TaxID=1805005 {ECO:0000313|EMBL:OIO88388.1, ECO:0000313|Proteomes:UP000182267};
RN [1] {ECO:0000313|EMBL:OIO88388.1, ECO:0000313|Proteomes:UP000182267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG2_30_64_16 {ECO:0000313|EMBL:OIO88388.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(2016).
CC -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3-
CC isopropylmalate, via the formation of 2-isopropylmaleate.
CC {ECO:0000256|HAMAP-Rule:MF_01027}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate;
CC Xref=Rhea:RHEA:32287, ChEBI:CHEBI:1178, ChEBI:CHEBI:35121;
CC EC=4.2.1.33; Evidence={ECO:0000256|HAMAP-Rule:MF_01027};
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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01027};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_01027};
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 2/4. {ECO:0000256|HAMAP-
CC Rule:MF_01027}.
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 2/2. {ECO:0000256|ARBA:ARBA00004717}.
CC -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000256|HAMAP-
CC Rule:MF_01027}.
CC -!- SIMILARITY: Belongs to the LeuD family. LeuD type 2 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01032}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. LeuC type 2
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01027}.
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:OIO88388.1}.
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DR EMBL; MNXL01000379; OIO88388.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J4ZP33; -.
DR UniPathway; UPA00048; UER00071.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000182267; Unassembled WGS sequence.
DR GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-UniRule.
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:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR CDD; cd01577; IPMI_Swivel; 1.
DR Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
DR HAMAP; MF_01027; LeuC_type2; 1.
DR HAMAP; MF_01032; LeuD_type2; 1.
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; IPR018136; Aconitase_4Fe-4S_BS.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR InterPro; IPR011826; HAcnase/IPMdehydase_lsu_prok.
DR InterPro; IPR033940; IPMI_Swivel.
DR InterPro; IPR011827; LeuD_type2/HacB/DmdB.
DR NCBIfam; TIGR02087; LEUD_arch; 1.
DR PANTHER; PTHR43822; HOMOACONITASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00330; Aconitase; 3.
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|HAMAP-Rule:MF_01027};
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01027};
KW Branched-chain amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01027};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01027};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_01027}; Leucine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01027};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01027};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01027}.
FT DOMAIN 25..170
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 191..332
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 333..462
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 594..654
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
FT REGION 472..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 346
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01027"
FT BINDING 411
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01027"
FT BINDING 414
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01027"
SQ SEQUENCE 727 AA; 77401 MW; 41B5AB5A2F8825F2 CRC64;
MGYTFAEKAL ARAAGLETTV AGQIVDARPD IVLSHDNTAA IARLFQDLGI ARIRHPERLA
VVLDHAVPAP NAEHARNHAE VRRFVAEQGI GHFFDAGRGI CHQVVSEEAL ILPGQTILGA
DSHTTHHGWL GAFGAGIGRS EVAALWATGE LWLRVPETIR VELTGDPSAA LRPFGEAQDR
LRSGQGSGQG LPPGVTAKDL SLYILGQLGP EAGIYQALEF GGPGLHTLSI ESRMVIPNMM
AEAGVKSAYL EPDGLVFEWL AERLGRRGKS RVLGGTEGNR NTVAGWRQRL AEGALYPDPD
ARYIARYTVN LNELEPMVAR PHKPDNSVPL SQIAGTHVDQ AFIGTCTNGR LEDLAAAATV
LRGPDGGVRH VAAGARLVVI PASSQVLQDA LAAGYVETFL AAGAMIGVPG CGPCMGNHLG
VPAADEVVIS SANRNFRGRM GNPESDIYLA SPAVVAASAV LGRIADPREI MGERQESGVR
SQESGVRGQG SGDRRQEAEV GGQEVRRIAG QPINQLAKQA IGESITQYPI PNTQYPIPNR
QSPIANTQFQ GRAWVYGDDV NTDVIFPGKY TYTVREEAEM ARHALEDLDP SFAAQVRPGD
IVVGGRNFGC GSSREQAVTC LRAAGVRALI AASFARIFYR NAIDNGVLPI TCPEAAAAIR
PGETISVDLD RCVVQCAAGE FPFQPLSPSV QQIFEAGGLL EMLRVIPNTK YPLPKASSTE
VICEQSV
//
