ID A0A016SQQ6_9BILA Unreviewed; 603 AA.
AC A0A016SQQ6;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=fumarate hydratase {ECO:0000256|ARBA:ARBA00012921};
DE EC=4.2.1.2 {ECO:0000256|ARBA:ARBA00012921};
GN Name=Acey_s0191.g1326 {ECO:0000313|EMBL:EYB92702.1};
GN Synonyms=Acey-fum-1 {ECO:0000313|EMBL:EYB92702.1};
GN ORFNames=Y032_0191g1326 {ECO:0000313|EMBL:EYB92702.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYB92702.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate
CC from fumarate: step 1/1. {ECO:0000256|ARBA:ARBA00004859}.
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:EYB92702.1}.
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DR EMBL; JARK01001527; EYB92702.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016SQQ6; -.
DR UniPathway; UPA00223; UER01007.
DR Proteomes; UP000024635; 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:UniProtKB-UniPathway.
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:UP000024635}.
FT DOMAIN 153..481
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 548..600
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 603 AA; 66001 MW; 163ECFA75122456E CRC64;
MIDFNRFNGC ITLLPPTKSS SFNVTAICVH IDACEKKNIN NGTYIAIHSQ RAVVLLSKGF
ITGSTRKVCQ NSTRPLNNSR VILQFNSMAN LQLIPIGLNL NVPLFHSNGS VYKDHGLKRT
EMRALYNYHL NHLAKWTIDP NAFQIRIERD AFGELEVPVD RYYGAATARA QTSFKIGGPE
ERMPLPVLHA FAIVKKASAM VNAEYGLDKK IADAICKAAD EIVAGKLDDH FPLNAWQTTT
HWNMNVNEVI ANRAIEMLGG VLGSKNPVHP NDHVNMAQST NDTYPSAMNI AVAREINSRL
FPALKQFRDS LQRKSNEFKD IIKIGRTHTQ DAVPITLGQE FSGYVQQVEN GIDRIRATLP
RLYQLVAGGT AVGTGLNTHK GFGEKVVKAI AADTGLPFTT TPNKFEATAA HDSLVEVHGA
LNTLAASLFK ICNDIRFLGS GPRCGLGELH LPENEPGSSI MPGKVNPTQC EALTMVAAQV
MANQVAVTIG GANGHFELNV CKPLMVKNNL QSVRLLSDVA VSFTVYCLDG ITANKERIAK
IMRESLMLVT ALNPHIGYDN ACKIAKTAHK NGTTLKEEAV KSGLVTPEQF DQWVRPEDMI
GPK
//