ID A0A1F3N9U7_9BACT Unreviewed; 422 AA.
AC A0A1F3N9U7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 22-FEB-2023, entry version 12.
DE RecName: Full=fumarate hydratase {ECO:0000256|ARBA:ARBA00012921};
DE EC=4.2.1.2 {ECO:0000256|ARBA:ARBA00012921};
DE Flags: Fragment;
GN Name=fumC {ECO:0000313|EMBL:OFY61854.1};
GN ORFNames=A2Y71_12860 {ECO:0000313|EMBL:OFY61854.1};
OS Bacteroidetes bacterium RBG_13_42_15.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1797355 {ECO:0000313|EMBL:OFY61854.1, ECO:0000313|Proteomes:UP000178321};
RN [1] {ECO:0000313|EMBL:OFY61854.1, ECO:0000313|Proteomes:UP000178321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OFY61854.1}.
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DR EMBL; MEOS01000292; OFY61854.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F3N9U7; -.
DR Proteomes; UP000178321; 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 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;
FT DOMAIN 4..302
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 368..421
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
FT REGION 81..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OFY61854.1"
SQ SEQUENCE 422 AA; 45188 MW; 36E6F1426332FA3A CRC64;
HEIIKAFGYI KKAAAITNFE LGILTSGKKD LIAAVCNEII EGKLDDQFPL VIWQTGSGTH
TNMNVNEVIA NRAHVKNGGV LSDNKKALHP NDDVNKSQSS NDTFPTAMHI AAYMVIKETT
LPGMQILRDA LARKSDEFRD VVKIGRTHLM DAVPLTLGQE ISGYVQQIDN GIRAIRNSLT
MVSELALGGS AVGTGLNIPT GYSDLVAKKI AELTGIPFVT APNKFESLAA HDAMVELSSA
LKRSAVSLMK IANDIRILSS GPRSGIGEII IPANEPGSSI MPGKVNPTQA EALSMVCAQI
IGNDVAVTIG NSGGNLELNT YKPLIAANVL QSARLLGEAC YSFSKNCIAG IQPDYDAIRN
HLNNSLMLVT ALSPYIGYDN CTRIAKKAFT EKITIRKAAL ELGLVSGDQF DKWVNPEKMT
GS
//
