ID Q8PWP8_METMA Unreviewed; 942 AA.
AC Q8PWP8;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 127.
DE RecName: Full=aconitate hydratase {ECO:0000256|ARBA:ARBA00012926};
DE EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
GN OrderedLocusNames=MM_1528 {ECO:0000313|EMBL:AAM31224.1};
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 {ECO:0000313|EMBL:AAM31224.1, ECO:0000313|Proteomes:UP000000595};
RN [1] {ECO:0000313|EMBL:AAM31224.1, ECO:0000313|Proteomes:UP000000595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88
RC {ECO:0000313|Proteomes:UP000000595};
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baumer S., Jacobi C.,
RA Bruggemann H., Lienard T., Christmann A., Bomeke 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 -!- 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|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185}.
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DR EMBL; AE008384; AAM31224.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8PWP8; -.
DR KEGG; mma:MM_1528; -.
DR PATRIC; fig|192952.21.peg.1764; -.
DR eggNOG; arCOG01697; Archaea.
DR HOGENOM; CLU_013476_1_0_2; -.
DR Proteomes; UP000000595; Chromosome.
DR GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd01586; AcnA_IRP; 1.
DR CDD; cd01580; AcnA_IRP_Swivel; 1.
DR Gene3D; 6.10.190.10; -; 1.
DR Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
DR InterPro; IPR044137; AcnA_IRP_Swivel.
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; IPR006249; Aconitase/IRP2.
DR InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR NCBIfam; TIGR01341; aconitase_1; 1.
DR PANTHER; PTHR11670; ACONITASE/IRON-RESPONSIVE ELEMENT FAMILY MEMBER; 1.
DR PANTHER; PTHR11670:SF54; CYTOPLASMIC ACONITATE HYDRATASE; 1.
DR Pfam; PF00330; Aconitase; 1.
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 Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Lyase {ECO:0000313|EMBL:AAM31224.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 83..603
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 733..868
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 942 AA; 103885 MW; 001EEAAAC72BFBBE CRC64;
MLEVKSKMRE GPDPFGVRDS IETTAGKATI YRLGKLEEKG FEGISLLPYS IRILLESLLR
HADTQKKTIT VEDVEALARW SPENISEKDI PFIPSRVIMQ DFTGVPAVVD LAALRSAMER
LGGDPAKINP VIPADLVIDH SVQVDSYGTA YSLGENEKKE FERNRERYTV LRWAQKAFDN
FRVVPPGRGI IHQVNLEYLT PLVHLSEKEG ELFAFPDTLV GTDSHTTMIN GIGVLGWGVG
GIEAEAVMLG QPYYMPVPEV VGFKLYGKLE PGVTATDLVL TITKMLRKHG VVGKFVEFYG
PGLNSLSLPD RATISNMAPE YGATLGIFPP DQETLDYMKR TGRSDEQVDL VKKYLEAQDL
LYSANKPEPV FSSNLELDMG TVKPCLAGPR RPQDQLFLNE VSENFCETMR QTFIRKKEGG
TDLARDPAYL RWIGEGGAPV EETEAQVARE TEKVGPVEKD FRVTHGSVVI ASITSCTNTS
NPSVLIGAGL LAKKAIERGL KVKPFVKTSL SPGSRVATEY LGAAGLLPYL EALGFHQVGY
GCTTCIGNSG PLPEHVSKEI EEKDLTVAAV LSGNRNFEGR INPLVKANYL ASPPLVVAYA
IAGTVNINFE TDPLAYDPNG IPVYLRDIWP MQDEIKQVEK ESVRPEMFKK EYSGVLEGAK
LWKELEVPEG TLYEWIPTST YIQEPPYFVD FPLTSPLLGD IRNARVLALF GDSITTDHIS
PAGDIPAESP AGRYLMSWGV DQKDFNSYGS RRGNHEVMMR GTFANIRLRN RLVSKEGGWT
VYHLKGEDFP PEACGEGMPI YDASLLYAEN NVPLIVIAGK EYGTGSSRDW AAKGTFLLGV
KAVIAESFER IHRSNLVGMG VLPLQFKAGE NADSLGLTGK ESYDILGIEK MEPHGELTVL
ARDDSGKETE FKATLRLDSA VEIEYYRNGG ILHKFLRDSV KK
//
