ID R9SJ38_9EURY Unreviewed; 161 AA.
AC R9SJ38;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Methanogen homoaconitase small subunit {ECO:0000256|HAMAP-Rule:MF_01032};
DE Short=HACN {ECO:0000256|HAMAP-Rule:MF_01032};
DE EC=4.2.1.114 {ECO:0000256|HAMAP-Rule:MF_01032};
DE AltName: Full=Homoaconitate hydratase {ECO:0000256|HAMAP-Rule:MF_01032};
GN Name=aksE {ECO:0000313|EMBL:AGN16415.1};
GN Synonyms=hacB {ECO:0000256|HAMAP-Rule:MF_01032};
GN ORFNames=Abm4_0514 {ECO:0000313|EMBL:AGN16415.1};
OS Methanobrevibacter sp. AbM4.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=224719 {ECO:0000313|EMBL:AGN16415.1, ECO:0000313|Proteomes:UP000014066};
RN [1] {ECO:0000313|EMBL:AGN16415.1, ECO:0000313|Proteomes:UP000014066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AbM4 {ECO:0000313|EMBL:AGN16415.1};
RA Leahy S.C., Kelly W.J., Li D., Lambie S.C., Altermann E., Li Y.,
RA Attwood G.T.;
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AGN16415.1, ECO:0000313|Proteomes:UP000014066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abm4 {ECO:0000313|Proteomes:UP000014066};
RG Pastoral Greenhouse Gas Research Consortium;
RA Leahy S.C., Kelly W.J., Li D., Lambie S.C., Altermann E., Li Y.,
RA Attwood G.T.;
RT "The comlpete genome sequence of Methanobrevibacter sp. AbM4.";
RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Hydro-lyase with broad substrate specificity for cis-
CC 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. All these reactions are part of the biosynthesis pathway of
CC coenzyme B. {ECO:0000256|HAMAP-Rule:MF_01032}.
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:0000256|HAMAP-Rule:MF_01032};
CC -!- PATHWAY: Organic acid metabolism; 2-oxosuberate biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_01032}.
CC -!- SUBUNIT: Heterotetramer of 2 HacA and 2 HacB proteins.
CC {ECO:0000256|HAMAP-Rule:MF_01032}.
CC -!- SIMILARITY: Belongs to the LeuD family. LeuD type 2 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01032}.
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DR EMBL; CP004050; AGN16415.1; -; Genomic_DNA.
DR RefSeq; WP_016358118.1; NC_021355.1.
DR AlphaFoldDB; R9SJ38; -.
DR STRING; 224719.Abm4_0514; -.
DR GeneID; 15798006; -.
DR KEGG; meb:Abm4_0514; -.
DR eggNOG; arCOG02230; Archaea.
DR HOGENOM; CLU_081378_1_1_2; -.
DR OrthoDB; 6505at2157; -.
DR UniPathway; UPA00919; -.
DR Proteomes; UP000014066; Chromosome.
DR GO; GO:0004409; F:homoaconitate hydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019298; P:coenzyme B biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd01577; IPMI_Swivel; 1.
DR Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
DR HAMAP; MF_01032; LeuD_type2; 1.
DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR InterPro; IPR033940; IPMI_Swivel.
DR InterPro; IPR011827; LeuD_type2/HacB/DmdB.
DR NCBIfam; NF040625; HacB2_Meth; 1.
DR NCBIfam; TIGR02087; LEUD_arch; 1.
DR PANTHER; PTHR43345:SF2; 3-ISOPROPYLMALATE DEHYDRATASE SMALL SUBUNIT 1-RELATED; 1.
DR PANTHER; PTHR43345; 3-ISOPROPYLMALATE DEHYDRATASE SMALL SUBUNIT 2-RELATED-RELATED; 1.
DR Pfam; PF00694; Aconitase_C; 1.
DR SUPFAM; SSF52016; LeuD/IlvD-like; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01032};
KW Reference proteome {ECO:0000313|Proteomes:UP000014066}.
FT DOMAIN 39..101
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
FT MOTIF 25..28
FT /note="YLRT"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01032"
FT SITE 27
FT /note="Critical for substrate specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01032"
SQ SEQUENCE 161 AA; 17940 MW; B1F694F8B5563E03 CRC64;
MEKIQGRVWT FGENIDTDLI IPGRYLRTFN PEDLAEHVLE GERPDFTHNV KKGDVIVADE
NFGCGSSREQ APVAIKAAGV DAIIAKSFAR IFYRNAINIG LPVIKADIKA SDEDIVSVDL
SEGIIRNETT GEDVEFEPFK DFMLEILEDG GLVNHYLKSK E
//
