HACA_METTH
ID HACA_METTH Reviewed; 428 AA.
AC O27668;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Probable methanogen homoaconitase large subunit;
DE Short=HACN;
DE EC=4.2.1.114 {ECO:0000250|UniProtKB:Q58409};
DE AltName: Full=Homoaconitate hydratase;
GN Name=hacA; OrderedLocusNames=MTH_1631;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
CC -!- FUNCTION: Component of a hydro-lyase with broad substrate specificity
CC for cis-unsaturated tricarboxylic acids. Catalyzes both the reversible
CC dehydration of (R)-homocitrate ((R)-2-hydroxybutane-1,2,4-
CC tricarboxylate) to produce cis-homoaconitate ((Z)-but-1-ene-1,2,4-
CC tricarboxylate), and its hydration to homoisocitrate ((1R,2S)-1-
CC hydroxybutane-1,2,4-tricarboxylate). Is also able to hydrate the
CC analogous longer chain substrates cis-homo(2)-aconitate, cis-homo(3)-
CC aconitate. These reactions are part of the biosynthesis pathway of
CC coenzyme B. {ECO:0000250|UniProtKB:Q58409}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-homocitrate = (2R,3S)-homoisocitrate;
CC Xref=Rhea:RHEA:32303, ChEBI:CHEBI:15404, ChEBI:CHEBI:58884;
CC EC=4.2.1.114; Evidence={ECO:0000250|UniProtKB:Q58409};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32304;
CC Evidence={ECO:0000250|UniProtKB:Q58409};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-homocitrate = cis-homoaconitate + H2O;
CC Xref=Rhea:RHEA:26101, ChEBI:CHEBI:15377, ChEBI:CHEBI:58174,
CC ChEBI:CHEBI:58884; Evidence={ECO:0000250|UniProtKB:Q58409};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26102;
CC Evidence={ECO:0000250|UniProtKB:Q58409};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,3S)-homoisocitrate = cis-homoaconitate + H2O;
CC Xref=Rhea:RHEA:15485, ChEBI:CHEBI:15377, ChEBI:CHEBI:15404,
CC ChEBI:CHEBI:58174; Evidence={ECO:0000250|UniProtKB:Q58409};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15487;
CC Evidence={ECO:0000250|UniProtKB:Q58409};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cis-(homo)2aconitate + H2O = (2R,3S)-iso(homo)2citrate;
CC Xref=Rhea:RHEA:68416, ChEBI:CHEBI:15377, ChEBI:CHEBI:72710,
CC ChEBI:CHEBI:72722; EC=4.2.1.114;
CC Evidence={ECO:0000250|UniProtKB:Q58409};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68417;
CC Evidence={ECO:0000250|UniProtKB:Q58409};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cis-(homo)3aconitate + H2O = (2R,3S)-iso(homo)3citrate;
CC Xref=Rhea:RHEA:68420, ChEBI:CHEBI:15377, ChEBI:CHEBI:72712,
CC ChEBI:CHEBI:177881; EC=4.2.1.114;
CC Evidence={ECO:0000250|UniProtKB:Q58409};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68421;
CC Evidence={ECO:0000250|UniProtKB:Q58409};
CC -!- PATHWAY: Organic acid metabolism; 2-oxosuberate biosynthesis.
CC {ECO:0000250|UniProtKB:Q58409}.
CC -!- SUBUNIT: Heterotetramer of 2 HacA and 2 HacB proteins.
CC {ECO:0000250|UniProtKB:Q58409}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. LeuC type 2
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01027}.
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DR EMBL; AE000666; AAB86104.1; -; Genomic_DNA.
DR PIR; A69085; A69085.
DR AlphaFoldDB; O27668; -.
DR SMR; O27668; -.
DR STRING; 187420.MTH_1631; -.
DR EnsemblBacteria; AAB86104; AAB86104; MTH_1631.
DR KEGG; mth:MTH_1631; -.
DR PATRIC; fig|187420.15.peg.1595; -.
DR HOGENOM; CLU_006714_3_4_2; -.
DR OMA; GIEHCLL; -.
DR UniPathway; UPA00919; -.
DR Proteomes; UP000005223; Chromosome.
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:0004409; F:homoaconitate hydratase activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd01583; IPMI; 1.
DR Gene3D; 3.30.499.10; -; 2.
DR HAMAP; MF_01027; LeuC_type2; 1.
DR InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR011826; HAcnase/IPMdehydase_lsu_prok.
DR InterPro; IPR006251; Homoacnase/IPMdehydase_lsu.
DR InterPro; IPR033941; IPMI_cat.
DR Pfam; PF00330; Aconitase; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; SSF53732; 1.
DR TIGRFAMs; TIGR01343; hacA_fam; 1.
DR TIGRFAMs; TIGR02086; IPMI_arch; 1.
DR PROSITE; PS00450; ACONITASE_1; 1.
DR PROSITE; PS01244; ACONITASE_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding; Reference proteome.
FT CHAIN 1..428
FT /note="Probable methanogen homoaconitase large subunit"
FT /id="PRO_0000076875"
FT BINDING 304
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01027"
FT BINDING 364
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01027"
FT BINDING 367
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01027"
SQ SEQUENCE 428 AA; 46448 MW; B93F1DC53C9B8178 CRC64;
MVKMNMTEKI LAEAAGLREV TPGEIIEARV DLAMTHDGTS PPTIRTFRDI ASRGGPARVW
DPERIVMVFD HNVPANTIGA AEFQRVTREF AREQGIVNIF QNAAGICHQV LPERGFVRPG
MVIVGADSHT CTYGAFGAFA TGMGATDMAM VFATGKTWFM VPEAMRIEVT GEPEGHVYAK
DVILHIIGEI GVDGATYRSV EFTGDTIESM DVSGRMTICN MAVEMGAKNG IMEPNRQTLD
YVRARTGREF RVYSSDEDSQ YLEDHHFDVS DLEPQVACPD DVDNVYPVHR VEGTHIDEAF
LGSCTNGRYE DLKIAAEVIG DRRVHEDVRF IVSPASREIY LKALEDGIIE TFIRAGAIVC
NPGCGPCLGA HMGVLAPGEV SIATTNRNFR GRMGDPASSV YLANPAVVAE SAIEGVISAP
QQEAGNGC
