ID A0A432ZRL1_9GAMM Unreviewed; 457 AA.
AC A0A432ZRL1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 03-MAY-2023, entry version 13.
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:RUO80466.1};
GN Synonyms=fumC {ECO:0000256|HAMAP-Rule:MF_00743};
GN ORFNames=CWI84_05260 {ECO:0000313|EMBL:RUO80466.1};
OS Idiomarina tyrosinivorans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Idiomarina.
OX NCBI_TaxID=1445662 {ECO:0000313|EMBL:RUO80466.1, ECO:0000313|Proteomes:UP000287996};
RN [1] {ECO:0000313|EMBL:RUO80466.1, ECO:0000313|Proteomes:UP000287996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-PW-9 {ECO:0000313|EMBL:RUO80466.1,
RC ECO:0000313|Proteomes:UP000287996};
RX PubMed=30364313; DOI=.3389/fmicb.2018.02453;
RA Liu Y., Lai Q., Shao Z.;
RT "Genome-Based Analysis Reveals the Taxonomy and Diversity of the Family
RT Idiomarinaceae.";
RL Front. Microbiol. 9:2453-2453(2018).
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 -!- 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:RUO80466.1}.
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DR EMBL; PIQH01000004; RUO80466.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A432ZRL1; -.
DR OrthoDB; 9802809at2; -.
DR UniPathway; UPA00223; UER01007.
DR Proteomes; UP000287996; 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-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:RUO80466.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000287996};
KW Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00743}.
FT DOMAIN 12..335
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 401..454
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
FT ACT_SITE 181
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT ACT_SITE 311
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 98..100
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 122..125
FT /ligand="substrate"
FT /note="in site B"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 132..134
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 180
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 312
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 317..319
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT SITE 324
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
SQ SEQUENCE 457 AA; 49290 MW; 6B8A0BA2B738754D CRC64;
MSEYRIETDS MGEVQVPHRA FYGAQTQRAV DNFAISGLTM PKQLIAAIAL IKHAAATANQ
EVAGLKASKA KAIRNVAKQI YEGQFADQFP IDIFQTGSGT SSNMNVNEVI AHLASSDDLN
VHPNDDVNCS QSSNDTIPTA IQLSAVLALK EHFAPALAHL IGRIKEKAGQ LQNHVKTGRT
HLMDAMPMTL AQELNSWAAQ LEVSQRQLPL LIEQLSELPQ GGTAIGTGIN APEQFAEHFS
RALSELTDHH FKPAENFFSG IAGQERSLAA SSLLNSIATT LLKISNDLRW MNSGPLAGLG
EIQLEALQPG SSIMPGKVNP VIPEAVAMVA AQVNGNHTTI TTAAQQGNFQ LNVMLPVIAY
NLLQSIEIVS TSCMHLADKA IQSFEVNQDR LDEALSKNPI LVTALNTEIG YNKAAEIAKR
AYKEKRPVLD VADEMTDLGR DKLAQLLDPK KLTKGGV
//