ID K9GQB6_PEND2 Unreviewed; 535 AA.
AC K9GQB6;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=fumarate hydratase {ECO:0000256|ARBA:ARBA00012921};
DE EC=4.2.1.2 {ECO:0000256|ARBA:ARBA00012921};
GN ORFNames=PDIG_27440 {ECO:0000313|EMBL:EKV15306.1};
OS Penicillium digitatum (strain PHI26 / CECT 20796) (Green mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1170229 {ECO:0000313|EMBL:EKV15306.1, ECO:0000313|Proteomes:UP000009882};
RN [1] {ECO:0000313|Proteomes:UP000009882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI26 / CECT 20796 {ECO:0000313|Proteomes:UP000009882};
RX PubMed=23171342; DOI=10.1186/1471-2164-13-646;
RA Marcet-Houben M., Ballester A.-R., de la Fuente B., Harries E.,
RA Marcos J.F., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome sequence of the necrotrophic fungus Penicillium digitatum, the main
RT postharvest pathogen of citrus.";
RL BMC Genomics 13:646-646(2012).
CC -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family. Fumarase
CC subfamily. {ECO:0000256|ARBA:ARBA00009084}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKV15306.1}.
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DR EMBL; AKCT01000122; EKV15306.1; -; Genomic_DNA.
DR AlphaFoldDB; K9GQB6; -.
DR STRING; 1170229.K9GQB6; -.
DR eggNOG; KOG1317; Eukaryota.
DR HOGENOM; CLU_021594_4_1_1; -.
DR InParanoid; K9GQB6; -.
DR OMA; AKWRAQT; -.
DR OrthoDB; 1341425at2759; -.
DR Proteomes; UP000009882; Unassembled WGS sequence.
DR GO; GO:0045239; C:tricarboxylic acid cycle enzyme complex; IEA:InterPro.
DR GO; GO:0004333; F:fumarate hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0006106; P:fumarate metabolic process; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR CDD; cd01362; Fumarase_classII; 1.
DR Gene3D; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1.
DR Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 1.
DR HAMAP; MF_00743; FumaraseC; 1.
DR InterPro; IPR005677; Fum_hydII.
DR InterPro; IPR024083; Fumarase/histidase_N.
DR InterPro; IPR018951; Fumarase_C_C.
DR InterPro; IPR020557; Fumarate_lyase_CS.
DR InterPro; IPR000362; Fumarate_lyase_fam.
DR InterPro; IPR022761; Fumarate_lyase_N.
DR InterPro; IPR008948; L-Aspartase-like.
DR NCBIfam; TIGR00979; fumC_II; 1.
DR PANTHER; PTHR11444; ASPARTATEAMMONIA/ARGININOSUCCINATE/ADENYLOSUCCINATE LYASE; 1.
DR PANTHER; PTHR11444:SF1; FUMARATE HYDRATASE, MITOCHONDRIAL; 1.
DR Pfam; PF10415; FumaraseC_C; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000009882}.
FT DOMAIN 80..411
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 477..529
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 535 AA; 57843 MW; FEAB7A8741BE3B77 CRC64;
MNPISSRAAV RSMATLTHAA RATPAARNVL SPFATRSLSS NARFTQFPRL QSLNTFSNKR
AFGTTVRMSV DTRTESDAFG EIQVPGDKYW GAQTQRSLGN FDINQPQDRM PAPVVKAFGI
LKGAAAEVNM KYGLDPKIGE AIKQAAAEVA EGKLLDHFPL VVWQTGSGTQ SNMNSNEVIS
NRAIEILGGT MGSKKPVHPN DHVNMSASSN DSFPTVMHIA AVVELEQSLL PSLKGLRDAL
QVKVDKFEHI IKIGRTHLQD ATPLTLGQEF SGYVAQLDRN IERVEATLPH LRFLAQGGTA
VGTGLNTFKG FDEAVAAEIS KLTGTEFKTA PNKFEVLAAH DSIIEASGSL NTLAASLFKI
AQDVRYLGSG PRCGLGELSL PENEPGSSIM PGKVNPTQCE SLTMVCAQVM GNHVAATIGG
MNGQFELNVF KPVMIANLLH SVRILSDGMN SFRTHLVEGL EANESRINSL LNESLMLVTC
LNPIIGYDMA SKVAKNAHKK NLTLKESAME LKALSSEEFD KYVRPELMLA PKELK
//
