ID A0A2P5BJE1_TREOI Unreviewed; 914 AA.
AC A0A2P5BJE1;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 13-SEP-2023, entry version 18.
DE RecName: Full=fumarate hydratase {ECO:0000256|ARBA:ARBA00012921};
DE EC=4.2.1.2 {ECO:0000256|ARBA:ARBA00012921};
GN ORFNames=TorRG33x02_319020 {ECO:0000313|EMBL:PON48912.1};
OS Trema orientale (Charcoal tree) (Celtis orientalis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Cannabaceae; Trema.
OX NCBI_TaxID=63057 {ECO:0000313|EMBL:PON48912.1, ECO:0000313|Proteomes:UP000237000};
RN [1] {ECO:0000313|Proteomes:UP000237000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. RG33-2 {ECO:0000313|Proteomes:UP000237000};
RA Van Velzen R., Holmer R., Bu F., Rutten L., Van Zeijl A., Liu W.,
RA Santuari L., Cao Q., Sharma T., Shen D., Roswanjaya Y., Wardhani T.,
RA Kalhor M.S., Jansen J., Van den Hoogen J., Gungor B., Hartog M.,
RA Hontelez J., Verver J., Yang W.-C., Schijlen E., Repin R., Schilthuizen M.,
RA Schranz E., Heidstra R., Miyata K., Fedorova E., Kohlen W., Bisseling T.,
RA Smit S., Geurts R.;
RT "Parallel loss of symbiosis genes in relatives of nitrogen-fixing non-
RT legume Parasponia.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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:PON48912.1}.
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DR EMBL; JXTC01000510; PON48912.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P5BJE1; -.
DR STRING; 63057.A0A2P5BJE1; -.
DR InParanoid; A0A2P5BJE1; -.
DR OrthoDB; 1341425at2759; -.
DR Proteomes; UP000237000; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 InterPro; IPR007320; PDCD2_C.
DR InterPro; IPR002893; Znf_MYND.
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 Pfam; PF04194; PDCD2_C; 1.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF144232; HIT/MYND zinc finger-like; 1.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
DR PROSITE; PS01360; ZF_MYND_1; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000237000};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00134}.
FT TRANSMEM 392..419
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 184..222
FT /note="MYND-type"
FT /evidence="ECO:0000259|PROSITE:PS50865"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..46
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 914 AA; 101331 MW; EAB628C66D7E3759 CRC64;
MAGASMRSDS MMEEFKGLRI TSLDEEDEDE EEEEEEDDDV DDDDQEANED VVLGFVKKPK
NPRSLFRHFF PSKAGGVPAW LDPVNLPSGR SFLCDICGEP LHFMLQVYAP EDVEYAFHRT
LFVFICTSMA CLRQDQHEQW KRHPNKPSRS VKVIRCQLPR DNPFYSSEPP KKDDKPSGAE
VPLCTWCGTW KGIKPCSSCQ KALYCSEKHR VKHSQLGHDY DCQRVRIASD SLDSGLIACT
SLWPELKIIQ EDESAFETEM SDDNGCSNSL VSRNRTDDTI MSLMKEFEGD DERKSWASFE
ERVSLAPEQV LRYCRTPGAK PLWPMSSGRP SKADIPKCNY CSGPLRFEFQ ILPQLLYYFR
VRNDVDSLDW ATIAVYTCEA SCDSNVAYKE EYAWLFGLSA VFLIGFPFLY SSLGTPLALA
MAMYTISRRL SSGGSTTLGT LRFAASWRFY SQSFREERDT FGPILVPSDK LWGAQTQRSL
QNFDIGGERE RMPEPIVRAF GILKKCAAKV NIEYGLDPSI GKAIMQAAQE VAEGKLNDHF
PLVVWQTGSG TQSNMNANEV IANRAAEILG HKRGEKFVHP NDHVNRSQSS NDTFPTVMHI
AAAMEINSRL LPNLKTLHTS LHSKSVEFKD IVKIGRTHTQ DATPLTLGQE FSGYTTQVKY
GIDRVLCTLP RMYQLAQGGT AVGTGLNTKK GFDEKIAAAV AEETSLPFVT AENKFEALAA
HDAFVETSGA LNTIAASLMK IANDIRLLGS GPRCGLGELI LPENEPGSSI MPGKVNPTQC
EALTMVCAQV FGNHVAITVG GANGHFELNV FKPVIANGLL HSLRLLGDAS ASFEKNCVRG
IQANRERIAK LLHESLMLVT SLNPKIGYDN AAAVAKKAHK EGTTLKEAAL NLRVLSSEEF
DNLVVPEKMI GPSD
//
