ID   Q8ZVT7_PYRAE            Unreviewed;       288 AA.
AC   Q8ZVT7;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   02-SEP-2026, entry version 87.
DE   SubName: Full=Fumarate hydratase class I alpha subunit {ECO:0000313|EMBL:AAL63969.1};
GN   OrderedLocusNames=PAE2132 {ECO:0000313|EMBL:AAL63969.1};
OS   Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS   104966 / NBRC 100827 / IM2).
OC   Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=178306 {ECO:0000313|EMBL:AAL63969.1, ECO:0000313|Proteomes:UP000002439};
RN   [1] {ECO:0000313|EMBL:AAL63969.1, ECO:0000313|Proteomes:UP000002439}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 /
RC   IM2 {ECO:0000313|Proteomes:UP000002439};
RX   PubMed=11792869; DOI=10.1073/pnas.241636498;
RA   Fitz-Gibbon S.T., Ladner H., Kim U.J., Stetter K.O., Simon M.I.,
RA   Miller J.H.;
RT   "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT   aerophilum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
CC   -!- SIMILARITY: Belongs to the class-I fumarase family.
CC       {ECO:0000256|ARBA:ARBA00008876}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE009441; AAL63969.1; -; Genomic_DNA.
DR   RefSeq; WP_011008437.1; NC_003364.1.
DR   AlphaFoldDB; Q8ZVT7; -.
DR   STRING; 178306.PAE2132; -.
DR   EnsemblBacteria; AAL63969; AAL63969; PAE2132.
DR   GeneID; 1464302; -.
DR   KEGG; pai:PAE2132; -.
DR   PATRIC; fig|178306.9.peg.1575; -.
DR   eggNOG; arCOG04407; Archaea.
DR   HOGENOM; CLU_041245_0_0_2; -.
DR   InParanoid; Q8ZVT7; -.
DR   Proteomes; UP000002439; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004333; F:fumarate hydratase activity; IBA:GO_Central.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR   InterPro; IPR051208; Class-I_Fumarase/Tartrate_DH.
DR   InterPro; IPR004646; Fe-S_hydro-lyase_TtdA-typ_cat.
DR   NCBIfam; NF004885; PRK06246.1; 1.
DR   NCBIfam; TIGR00722; ttdA_fumA_fumB; 1.
DR   PANTHER; PTHR30389; FUMARATE HYDRATASE-RELATED; 1.
DR   PANTHER; PTHR30389:SF17; L(+)-TARTRATE DEHYDRATASE SUBUNIT ALPHA-RELATED; 1.
DR   Pfam; PF05681; Fumerase; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002439}.
FT   DOMAIN          9..277
FT                   /note="Fe-S hydro-lyase tartrate dehydratase alpha-type
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF05681"
SQ   SEQUENCE   288 AA;  31037 MW;  C24F00724208A2E3 CRC64;
     MLEAVLLKAA KEVVARASVG PALDINNALK KAYEIEEGEA AKLQLGAILK NIELSISENA
     AVCQDTGFPN FYIKLGDRFP IRSKIYDILT QAVREVTKGL PLRPNTVHPF TEKNPGDNTG
     VGAPWFEVEL FDGDYVEFYY VPKGGGTELP SKAFTLPPGV AMKELPRLVL EAVIDAGPMP
     CPPVIVGVGV GPSVDIAAKL AKKAAVLRPV GSRHPEPEIA KMEEELLKAI NKLGIGVHGV
     GGKVTALDVH IEYAYRHPAA FSIGIVFSCW ATRRAGARVY PDGRYELL
//