ID A0A099D0X6_9ACTN Unreviewed; 465 AA.
AC A0A099D0X6;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Fumarate hydratase class II {ECO:0000256|HAMAP-Rule:MF_00743};
DE Short=Fumarase C {ECO:0000256|HAMAP-Rule:MF_00743};
DE EC=4.2.1.2 {ECO:0000256|HAMAP-Rule:MF_00743};
DE AltName: Full=Aerobic fumarase {ECO:0000256|HAMAP-Rule:MF_00743};
DE AltName: Full=Iron-independent fumarase {ECO:0000256|HAMAP-Rule:MF_00743};
GN Name=aspA {ECO:0000313|EMBL:ASU79874.1};
GN Synonyms=fumC {ECO:0000256|HAMAP-Rule:MF_00743};
GN ORFNames=CDG81_18205 {ECO:0000313|EMBL:ASU79874.1}, IL38_21840
GN {ECO:0000313|EMBL:KGI79694.1};
OS Actinopolyspora erythraea.
OC Bacteria; Actinomycetota; Actinomycetes; Actinopolysporales;
OC Actinopolysporaceae; Actinopolyspora.
OX NCBI_TaxID=414996 {ECO:0000313|EMBL:ASU79874.1, ECO:0000313|Proteomes:UP000215043};
RN [1] {ECO:0000313|EMBL:KGI79694.1, ECO:0000313|Proteomes:UP000029737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM90600 {ECO:0000313|EMBL:KGI79694.1,
RC ECO:0000313|Proteomes:UP000029737};
RX PubMed=25250723;
RA Chen D., Feng J., Huang L., Zhang Q., Wu J., Zhu X., Duan Y., Xu Z.;
RT "Identification and Characterization of a New Erythromycin Biosynthetic
RT Gene Cluster in Actinopolyspora erythraea YIM90600, a Novel Erythronolide-
RT Producing Halophilic Actinomycete Isolated from Salt Field.";
RL PLoS ONE 9:E108129-E108129(2014).
RN [2] {ECO:0000313|EMBL:ASU79874.1, ECO:0000313|Proteomes:UP000215043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 90600 {ECO:0000313|EMBL:ASU79874.1,
RC ECO:0000313|Proteomes:UP000215043};
RA Yin M., Tang S.;
RT "The complete genome sequence of moderately halophilic actinomycete
RT Actinopolyspora erythraea YIM 90600, the producer of novel erythromycin,
RT novel actinopolysporins A-C and tubercidin.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the TCA cycle. Catalyzes the stereospecific
CC interconversion of fumarate to L-malate. {ECO:0000256|HAMAP-
CC Rule:MF_00743}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malate = fumarate + H2O; Xref=Rhea:RHEA:12460,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15589, ChEBI:CHEBI:29806; EC=4.2.1.2;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00743};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate
CC from fumarate: step 1/1. {ECO:0000256|HAMAP-Rule:MF_00743}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00743}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00743}.
CC -!- MISCELLANEOUS: There are 2 substrate-binding sites: the catalytic A
CC site, and the non-catalytic B site that may play a role in the transfer
CC of substrate or product between the active site and the solvent.
CC Alternatively, the B site may bind allosteric effectors.
CC {ECO:0000256|HAMAP-Rule:MF_00743}.
CC -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family. Fumarase
CC subfamily. {ECO:0000256|ARBA:ARBA00009084, ECO:0000256|HAMAP-
CC Rule:MF_00743}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP022752; ASU79874.1; -; Genomic_DNA.
DR EMBL; JPMV01000040; KGI79694.1; -; Genomic_DNA.
DR RefSeq; WP_043578441.1; NZ_KN214180.1.
DR AlphaFoldDB; A0A099D0X6; -.
DR KEGG; aey:CDG81_18205; -.
DR eggNOG; COG0114; Bacteria.
DR HOGENOM; CLU_021594_4_1_11; -.
DR OrthoDB; 9802809at2; -.
DR UniPathway; UPA00223; UER01007.
DR Proteomes; UP000029737; Unassembled WGS sequence.
DR Proteomes; UP000215043; Chromosome.
DR GO; GO:0045239; C:tricarboxylic acid cycle enzyme complex; IEA:InterPro.
DR GO; GO:0004333; F:fumarate hydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006106; P:fumarate metabolic process; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
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 Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00743};
KW Lyase {ECO:0000256|HAMAP-Rule:MF_00743, ECO:0000313|EMBL:ASU79874.1};
KW Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00743}.
FT DOMAIN 14..338
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 404..461
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
FT ACT_SITE 184
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT ACT_SITE 314
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 100..102
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 125..128
FT /ligand="substrate"
FT /note="in site B"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 135..137
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 315
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 320..322
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT SITE 327
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
SQ SEQUENCE 465 AA; 49473 MW; 120A13731A6474BD CRC64;
MSEQRYRTEH DTMGEVQVPA EALYRAQTQR AVDNFPVSGQ GLERAQIRAL GLLKAATARV
NGRLGVLEAD MAEAIAAAAD EVAEGRHDDH FPIDVFQTGS GTSSNMNANE VIATLATRSL
GRDVHPNDHV NASQSSNDTF PTTIHVAATE AVLTDTIPAL EQLAAVIEDR AAQWSEVVKS
GRTHLMDAVP ITLGQEAGAW AAQARYGVER LRAGLDRLGE LPIGGTAVGS GLNAPEGFGA
AVSSELARVT GLPLTEARDH FEAQATQDGV VETSGNLRTV AVSLNKIAND LRWLGSGPRT
GLAELALPDL QPGSSIMPGK VNPVIPEATM QVVAQVVGND ATVSFAGSQG NFQLNVNLPV
IARNVLESAR LLAAVSRLLA DKVFAGVEVD TERAREYAEG SPSIVTPLNR YIGYEEAAAV
AKQALKERKT IREVVLERGY VEEGKLTRQQ LDEALDVLSM ARADR
//
