ID A0A0R0AQD9_9GAMM Unreviewed; 464 AA.
AC A0A0R0AQD9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=fumarate hydratase {ECO:0000256|ARBA:ARBA00012921};
DE EC=4.2.1.2 {ECO:0000256|ARBA:ARBA00012921};
DE Flags: Fragment;
GN Name=aspA {ECO:0000313|EMBL:KRG47452.1};
GN ORFNames=ARC20_17700 {ECO:0000313|EMBL:KRG47452.1};
OS Stenotrophomonas panacihumi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=676599 {ECO:0000313|EMBL:KRG47452.1, ECO:0000313|Proteomes:UP000051802};
RN [1] {ECO:0000313|EMBL:KRG47452.1, ECO:0000313|Proteomes:UP000051802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 16536 {ECO:0000313|EMBL:KRG47452.1,
RC ECO:0000313|Proteomes:UP000051802};
RA Patil P.P., Midha S., Patil P.B.;
RT "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL Submitted (OCT-2015) 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:KRG47452.1}.
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DR EMBL; LLXU01000034; KRG47452.1; -; Genomic_DNA.
DR RefSeq; WP_057643250.1; NZ_LLXU01000034.1.
DR AlphaFoldDB; A0A0R0AQD9; -.
DR STRING; 676599.ARC20_17700; -.
DR OrthoDB; 9802809at2; -.
DR Proteomes; UP000051802; 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:SF22; FUMARATE HYDRATASE CLASS II; 1.
DR Pfam; PF10415; FumaraseC_C; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00145; ARGSUCLYASE.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:KRG47452.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051802}.
FT DOMAIN 13..340
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 406..458
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
FT NON_TER 464
FT /evidence="ECO:0000313|EMBL:KRG47452.1"
SQ SEQUENCE 464 AA; 48915 MW; DD67367396F4F0A1 CRC64;
MSDKYRTEHD SMGELQVPAD ALWGAQTQRA VQNFPVSGQR MPRGFIRALG LVKGAAAQAN
AELGLLPKGV AKAVQQAAAE VAEGEHDAHF PIDVYQTGSG TSSNMNANEV IATLATRLLK
GGKAKVHPND HVNLGQSSND VIPTAIRVSA QLATVEQLLP ALKHLRKTID KRAKGLGKVV
KTGRTHLMDA MPLTFAQEFG AWSAQIASSE ARIEDALKRL RRLPLGGTAI GTGINADARF
GGKVAKLLSG STGTRFESAE NKFEGLAAQD DAVELSGQLN ATAVALIKIA NDLRWMNAGP
LAGLGEIVLP ALQPGSSIMP GKVNPVIPEA TVMACAQVIG HHTAITVAGQ TGNFQLNVTL
PLIALNLLDS IGLLANVSRL LADSAIAGLK VRQDRVREAL DRNPILVTAL NPIIGYEKAA
AIAKRAYKEN RPVLDVARED SGLPEAELKR LLDPGALTRG GIQA
//
