HACA_METAC
ID HACA_METAC Reviewed; 424 AA.
AC Q8TLF1;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 123.
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; Synonyms=leuC; OrderedLocusNames=MA_3085;
OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS C2A).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=188937;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX PubMed=11932238; DOI=10.1101/gr.223902;
RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT physiological diversity.";
RL Genome Res. 12:532-542(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; AE010299; AAM06458.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8TLF1; -.
DR SMR; Q8TLF1; -.
DR STRING; 188937.MA_3085; -.
DR EnsemblBacteria; AAM06458; AAM06458; MA_3085.
DR KEGG; mac:MA_3085; -.
DR HOGENOM; CLU_006714_3_4_2; -.
DR InParanoid; Q8TLF1; -.
DR OMA; GIEHCLL; -.
DR PhylomeDB; Q8TLF1; -.
DR UniPathway; UPA00919; -.
DR Proteomes; UP000002487; 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..424
FT /note="Probable methanogen homoaconitase large subunit"
FT /id="PRO_0000076866"
FT BINDING 308
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01027"
FT BINDING 366
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01027"
FT BINDING 369
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01027"
SQ SEQUENCE 424 AA; 45377 MW; 4588A59C5A8D43FE CRC64;
MLFDYRKGGL FLGTISEKIF SRAAGTEAKA NDFVLADVDY AMAHDGTSVL AVNAFKEMEM
EKVWDPSRIV VPFDHIAPAN NETSATLQRE IREWVKEQGI PNFYEVGEGI CHQVLPENGF
ALPGKLVVGA DSHSCTYGAF GAFATGVGAT DMAEIFATGK LWFKVPESFR MTVEGSLRKG
VYAKDLTLYL IGKTGIAGAT YKAVEFYGQA IRELTVAGRM TLCNMAIEMG AKTGIVPPDE
KTFEFLKNRA AATYEPVYAD PDAVYLEEFT YDADDIEPQV ACPHQVDNVK PVGEVEGTHV
DQVFIGTCTN GRLEDLEVAA AVLKGKQVAV RTIVIPASRT TLLAAIENGT METLLKAGVT
LATPGCGPCL GAHQGVLGEG EVCVSTANRN FKGRMGKGGF IYLASPATAA ASALTGEITD
PRTV
