HACA_METMA
ID HACA_METMA Reviewed; 391 AA.
AC Q8PZT3;
DT 06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 133.
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=MM_0409;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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; AE008384; AAM30105.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8PZT3; -.
DR SMR; Q8PZT3; -.
DR STRING; 192952.MM_0409; -.
DR PRIDE; Q8PZT3; -.
DR EnsemblBacteria; AAM30105; AAM30105; MM_0409.
DR KEGG; mma:MM_0409; -.
DR PATRIC; fig|192952.21.peg.491; -.
DR eggNOG; arCOG01698; Archaea.
DR HOGENOM; CLU_006714_3_4_2; -.
DR OMA; GIEHCLL; -.
DR UniPathway; UPA00919; -.
DR Proteomes; UP000000595; 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..391
FT /note="Probable methanogen homoaconitase large subunit"
FT /id="PRO_0000076872"
FT BINDING 275
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01027"
FT BINDING 333
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01027"
FT BINDING 336
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01027"
SQ SEQUENCE 391 AA; 41938 MW; 9AE2E29FFD94070F CRC64;
MLADVDYAMA HDGTSILAVN AFKEMEMERV WDPSRIVIPF DHIAPANTET SATLQKEIRE
WVREQSIPNF YEIGEGICHQ VLPENGFALP GKLLVGADSH SCTYGAFGAF ATGVGATDMA
EIFATGKLWF KVPESFRMTV EGSLDKHVYA KDLTLYLIGK TGIAGATYKA VEFYGQAISE
LSVAGRMTLC NMAIEMGAKT GIVPPDEKTF DFLKNRAVAP YEPVYSDPDA SYLKEFVYDA
GDIEPQVACP HQVDNVKPVG EVEGTHVDQV FIGTCTNGRL EDLEVAASVL KGKKVTVRTI
IIPASRSTLL AAIKNGTMEI LLKAGVTLAT PGCGPCLGAH QGVLGEGEVC VSTANRNFKG
RMGKDGFIYL ASPATAAASA LTGEITDPRK I
